Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Serum albumin

 ALBU_HUMAN              Reviewed;         609 AA.
P02768; E7ESS9; O95574; P04277; Q13140; Q645G4; Q68DN5; Q6UXK4;
Q86YG0; Q8IUK7; Q9P157; Q9P1I7; Q9UHS3; Q9UJZ0;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 2.
30-AUG-2017, entry version 243.
RecName: Full=Serum albumin;
Flags: Precursor;
Name=ALB;
ORFNames=GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675,
UNQ696/PRO1341;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-420.
PubMed=6171778; DOI=10.1093/nar/9.22.6103;
Lawn R.M., Adelman J., Bock S.C., Franke A.E., Houck C.M.,
Najarian R.C., Seeburg P.H., Wion K.L.;
"The sequence of human serum albumin cDNA and its expression in E.
coli.";
Nucleic Acids Res. 9:6103-6114(1981).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-121.
PubMed=6275391; DOI=10.1073/pnas.79.1.71;
Dugaiczyk A., Law S.W., Dennison O.E.;
"Nucleotide sequence and the encoded amino acids of human serum
albumin mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 79:71-75(1982).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3009475;
Minghetti P.P., Ruffner D.E., Kuang W.J., Dennison O.E., Hawkins J.W.,
Beattie W.G., Dugaiczyk A.;
"Molecular structure of the human albumin gene is revealed by
nucleotide sequence within q11-22 of chromosome 4.";
J. Biol. Chem. 261:6747-6757(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Yang S., Zhang R.A., Qi Z.W., Yuan Z.Y.;
"Human serum albumin.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIROSHIMA-1
LYS-378.
Huang M.C., Wu H.T.;
"The cDNA sequences of human serum albumin.";
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hinchliffe E.;
"Induction of galactose regulated gene expression in yeast.";
Patent number EP0248637, 09-DEC-1987.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Yu Z., Fu Y.;
"High expression HSA in Pichia for Pharmaceutical Use.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wang F., Huang L.;
"Cloning and sequence analysis of human albumin gene.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Kim J.W.;
"Identification of a human cell growth inhibition gene.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=11483580; DOI=10.1101/gr.175501;
Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C.,
Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C.,
He F.;
"Gene expression profiling in human fetal liver and identification of
tissue- and developmental-stage-specific genes through compiled
expression profiles and efficient cloning of full-length cDNAs.";
Genome Res. 11:1392-1403(2001).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TYR-27.
TISSUE=Liver;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Liver, and Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-455.
TISSUE=Liver;
Menaya J., Parrilla R., Ayuso M.S.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
PubMed=2419329;
Urano Y., Watanabe K., Sakai M., Tamaoki T.;
"The human albumin gene. Characterization of the 5' and 3' flanking
regions and the polymorphic gene transcripts.";
J. Biol. Chem. 261:3244-3251(1986).
[19]
PROTEIN SEQUENCE OF 25-609.
PubMed=1225573; DOI=10.1016/0014-5793(75)80242-0;
Meloun B., Moravek L., Kostka V.;
"Complete amino acid sequence of human serum albumin.";
FEBS Lett. 58:134-137(1975).
[20]
PROTEIN SEQUENCE OF 25-609.
Brown J.R., Shockley P., Behrens P.Q.;
(In) Bing D.H. (eds.);
The chemistry and physiology of the human plasma proteins, pp.23-40,
Pergamon Press, New York (1979).
[21]
PROTEIN SEQUENCE OF 25-44 AND 480-499.
TISSUE=Heart;
PubMed=7895732; DOI=10.1002/elps.11501501209;
Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
"The human myocardial two-dimensional gel protein database: update
1994.";
Electrophoresis 15:1459-1465(1994).
[22]
PROTEIN SEQUENCE OF 25-34.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[23]
PROTEIN SEQUENCE OF 45-75; 98-130; 162-183; 239-254; 265-281; 287-298;
348-372; 397-434; 438-452; 500-543; 550-558; 570-581 AND 599-609, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[24]
PROTEIN SEQUENCE OF 166-174.
PubMed=3087352; DOI=10.1016/0006-291X(86)90429-8;
Mogard M.H., Kobayashi R., Chen C.F., Lee T.D., Reeve J.R. Jr.,
Shively J.E., Walsh J.H.;
"The amino acid sequence of kinetensin, a novel peptide isolated from
pepsin-treated human plasma: homology with human serum albumin,
neurotensin and angiotensin.";
Biochem. Biophys. Res. Commun. 136:983-988(1986).
[25]
PROTEIN SEQUENCE OF 166-174.
PubMed=2437111;
Carraway R.E., Mitra S.P., Cochrane D.E.;
"Structure of a biologically active neurotensin-related peptide
obtained from pepsin-treated albumin(s).";
J. Biol. Chem. 262:5968-5973(1987).
[26]
PROTEIN SEQUENCE OF 222-229, AND ASPIRIN-ACETYLATION AT LYS-223.
PubMed=955075; DOI=10.1016/0014-5793(76)80496-6;
Walker J.E.;
"Lysine residue 199 of human serum albumin is modified by
acetylsalicylic acid.";
FEBS Lett. 66:173-175(1976).
[27]
PROTEIN SEQUENCE OF 250-264, GLYCATION AT LYS-75; LYS-161; LYS-186;
LYS-249; LYS-257; LYS-300; LYS-337; LYS-347; LYS-375; LYS-402;
LYS-437; LYS-468; LYS-560; LYS-549; LYS-569 AND LYS-597, LACK OF
GLYCATION AT LYS-28; LYS-44; LYS-65; LYS-88; LYS-97; LYS-117; LYS-130;
LYS-160; LYS-183; LYS-198; LYS-205; LYS-214; LYS-219; LYS-229;
LYS-236; LYS-264; LYS-286; LYS-298; LYS-310; LYS-383; LYS-396;
LYS-413; LYS-426; LYS-438; LYS-456; LYS-460; LYS-490; LYS-499;
LYS-524; LYS-543; LYS-548; LYS-562; LYS-565; LYS-581; LYS-584; LYS-588
AND LYS-598, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15047055; DOI=10.1016/j.jasms.2003.11.014;
Lapolla A., Fedele D., Reitano R., Arico N.C., Seraglia R., Traldi P.,
Marotta E., Tonani R.;
"Enzymatic digestion and mass spectrometry in the study of advanced
glycation end products/peptides.";
J. Am. Soc. Mass Spectrom. 15:496-509(2004).
[28]
DISULFIDE BONDS.
Saber M.A., Stockbauer P., Moravek L., Meloun B.;
"Disulfide bonds in human serum albumin.";
Collect. Czech. Chem. Commun. 42:564-579(1977).
[29]
BILIRUBIN-BINDING SITE.
PubMed=656055; DOI=10.1042/bj1710453;
Jacobsen C.;
"Lysine residue 240 of human serum albumin is involved in high-
affinity binding of bilirubin.";
Biochem. J. 171:453-459(1978).
[30]
GLYCATION AT LYS-223 AND LYS-549.
PubMed=6853480;
Garlick R.L., Mazer J.S.;
"The principal site of nonenzymatic glycosylation of human serum
albumin in vivo.";
J. Biol. Chem. 258:6142-6146(1983).
[31]
GLYCATION AT LYS-549.
PubMed=6706980;
Shaklai N., Garlick R.L., Bunn H.F.;
"Nonenzymatic glycosylation of human serum albumin alters its
conformation and function.";
J. Biol. Chem. 259:3812-3817(1984).
[32]
GLYCATION AT LYS-36; LYS-223; LYS-257; LYS-305; LYS-341; LYS-375;
LYS-463; LYS-549 AND LYS-558.
PubMed=3759977;
Iberg N., Fluckiger R.;
"Nonenzymatic glycosylation of albumin in vivo. Identification of
multiple glycosylated sites.";
J. Biol. Chem. 261:13542-13545(1986).
[33]
INVOLVEMENT IN ANALBA.
PubMed=8134387; DOI=10.1073/pnas.91.6.2275;
Watkins S., Madison J., Galliano M., Minchiotti L., Putnam F.W.;
"A nucleotide insertion and frameshift cause analbuminemia in an
Italian family.";
Proc. Natl. Acad. Sci. U.S.A. 91:2275-2279(1994).
[34]
FUNCTION, AND ZINC-BINDING SITES.
PubMed=19021548; DOI=10.1042/BST0361317;
Lu J., Stewart A.J., Sadler P.J., Pinheiro T.J., Blindauer C.A.;
"Albumin as a zinc carrier: properties of its high-affinity zinc-
binding site.";
Biochem. Soc. Trans. 36:1317-1321(2008).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; THR-444 AND
THR-446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89 AND SER-513,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-558, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[40]
PHOSPHORYLATION AT SER-29; SER-82; SER-89 AND THR-107.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[42]
X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
PubMed=2727704; DOI=10.1126/science.2727704;
Carter D.C., He X.-M., Munson S.H., Twigg P.D., Gernert K.M.,
Broom M.B., Miller T.Y.;
"Three-dimensional structure of human serum albumin.";
Science 244:1195-1198(1989).
[43]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).
PubMed=2374930; DOI=10.1126/science.2374930;
Carter D.C., He X.-M.;
"Structure of human serum albumin.";
Science 249:302-303(1990).
[44]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=1630489; DOI=10.1038/358209a0;
He X.-M., Carter D.C.;
"Atomic structure and chemistry of human serum albumin.";
Nature 358:209-215(1992).
[45]
ERRATUM.
He X.-M., Carter D.C.;
Nature 364:362-362(1993).
[46]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=9731778; DOI=10.1038/1869;
Curry S., Mandelkow H., Brick P., Franks N.;
"Crystal structure of human serum albumin complexed with fatty acid
reveals an asymmetric distribution of binding sites.";
Nat. Struct. Biol. 5:827-835(1998).
[47]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=10388840; DOI=10.1093/protein/12.6.439;
Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K.;
"Crystal structure of human serum albumin at 2.5-A resolution.";
Protein Eng. 12:439-446(1999).
[48]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-609.
PubMed=10940303; DOI=10.1074/jbc.M005460200;
Bhattacharya A.A., Curry S., Franks N.P.;
"Binding of the general anesthetics propofol and halothane to human
serum albumin. High resolution crystal structures.";
J. Biol. Chem. 275:38731-38738(2000).
[49]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=11743713; DOI=10.1006/jmbi.2000.5208;
Petitpas I., Grune T., Bhattacharya A.A., Curry S.;
"Crystal structures of human serum albumin complexed with
monounsaturated and polyunsaturated fatty acids.";
J. Mol. Biol. 314:955-960(2001).
[50]
VARIANT CANTERBURY ASN-337.
PubMed=3828358; DOI=10.1016/0167-4838(87)90088-4;
Brennan S.O., Herbert P.;
"Albumin Canterbury (313 Lys-->Asn). A point mutation in the second
domain of serum albumin.";
Biochim. Biophys. Acta 912:191-197(1987).
[51]
VARIANTS NASKAPI/MERSIN GLU-396 AND MEXICO GLY-574.
PubMed=3474609; DOI=10.1073/pnas.84.13.4413;
Takahashi N., Takahashi Y., Blumberg B.S., Putnam F.W.;
"Amino acid substitutions in genetic variants of human serum albumin
and in sequences inferred from molecular cloning.";
Proc. Natl. Acad. Sci. U.S.A. 84:4413-4417(1987).
[52]
VARIANTS NAGASAKI-3 GLN-27 YANOMAMA-2 GLU-396; NAGASAKI-2 ASN-399 AND
MAKU GLU-565.
PubMed=3479777; DOI=10.1073/pnas.84.22.8001;
Takshashi N., Takahashi Y., Isobe T., Putnam F.W., Fujita M.,
Satoh C., Neel J.V.;
"Amino acid substitutions in inherited albumin variants from
Amerindian and Japanese populations.";
Proc. Natl. Acad. Sci. U.S.A. 84:8001-8005(1987).
[53]
VARIANTS FUKUOKA-2 HIS-23; CHRISTCHURCH/HONOLULU-2 GLN-24; TAGLIACOZZO
ASN-337 AND ALBUMIN B/OSAKA-2/PHNOM PHEN LYS-594.
PubMed=2911589; DOI=10.1073/pnas.86.2.434;
Arai K., Ishioka N., Huss K., Madison J., Putnam F.W.;
"Identical structural changes in inherited albumin variants from
different populations.";
Proc. Natl. Acad. Sci. U.S.A. 86:434-438(1989).
[54]
VARIANTS HONOLULU-2 GLN-24; NAGASAKI-1 GLY-293; HIROSHIMA-1 LYS-378;
TOCHIGI LYS-400; HIROSHIMA-2 LYS-406 AND OSAKA-2 LYS-594.
PubMed=2762316; DOI=10.1073/pnas.86.16.6092;
Arai K., Madison J., Huss K., Ishioka N., Satoh C., Fujita M.,
Neel J.V., Sakurabayashi I., Putnam F.W.;
"Point substitutions in Japanese alloalbumins.";
Proc. Natl. Acad. Sci. U.S.A. 86:6092-6096(1989).
[55]
VARIANTS HONOLULU-1 PRO-24; HONOLULU-2 GLN-24; NAGOYA LYS-143; NEW
GUINEA ASN-337; MANAUS-1/LAMBADI LYS-525; FUKUOKA-1 ASN-587; OSAKA-1
LYS-589 AND OSAKA-2 LYS-594.
PubMed=2404284; DOI=10.1073/pnas.87.1.497;
Arai K., Madison J., Shimuzu A., Putnam F.W.;
"Point substitutions in albumin genetic variants from Asia.";
Proc. Natl. Acad. Sci. U.S.A. 87:497-501(1990).
[56]
CHARACTERIZATION OF VARIANT REDHILL.
PubMed=2104980; DOI=10.1073/pnas.87.1.26;
Brennan S.O., Myles T., Peach R.J., Donaldson D., George P.M.;
"Albumin Redhill (-1 Arg, 320 Ala-->Thr): a glycoprotein variant of
human serum albumin whose precursor has an aberrant signal peptidase
cleavage site.";
Proc. Natl. Acad. Sci. U.S.A. 87:26-30(1990).
[57]
VARIANTS VARESE HIS-23; TORINO LYS-84 AND VIBO VALENTIA LYS-106.
PubMed=2247440; DOI=10.1073/pnas.87.22.8721;
Galliano M., Minchiotti L., Porta F., Rossi A., Ferri G., Madison J.,
Watkins S., Putnam F.W.;
"Mutations in genetic variants of human serum albumin found in
Italy.";
Proc. Natl. Acad. Sci. U.S.A. 87:8721-8725(1990).
[58]
CHARACTERIZATION OF VARIANT VENEZIA.
PubMed=2068071; DOI=10.1073/pnas.88.14.5959;
Watkins S., Madison J., Davis E., Sakamoto Y., Galliano M.,
Minchiotti L., Putnam F.W.;
"A donor splice mutation and a single-base deletion produce two
carboxyl-terminal variants of human serum albumin.";
Proc. Natl. Acad. Sci. U.S.A. 88:5959-5963(1991).
[59]
VARIANTS KOMAGOME-3 HIS-23; IOWA CITY-2 VAL-25; KOMAGOME-2 ARG-152;
IOWA CITY-1 VAL-389 AND KOMAGOME-1 GLU-396.
PubMed=1946412; DOI=10.1073/pnas.88.21.9853;
Madison J., Arai K., Feld R.D., Kyle R.A., Watkins S., Davis E.,
Matsuda Y., Amaki I., Putnam F.W.;
"Genetic variants of serum albumin in Americans and Japanese.";
Proc. Natl. Acad. Sci. U.S.A. 88:9853-9857(1991).
[60]
VARIANT CASEBROOK ASN-518.
PubMed=1859851; DOI=10.1016/0925-4439(91)90023-3;
Peach R.J., Brennan S.O.;
"Structural characterization of a glycoprotein variant of human serum
albumin: albumin Casebrook (494 Asp-->Asn).";
Biochim. Biophys. Acta 1097:49-54(1991).
[61]
VARIANTS SONDRIO LYS-357 AND PARIS-2 ASN-587.
PubMed=1347703; DOI=10.1016/0167-4838(92)90207-T;
Minchiotti L., Galliano M., Stoppini M., Ferri G., Crespeau H.,
Rochu D., Porta F.;
"Two alloalbumins with identical electrophoretic mobility are produced
by differently charged amino acid substitutions.";
Biochim. Biophys. Acta 1119:232-238(1992).
[62]
VARIANTS MALMO-I CYS-23; MALMO-95 ASN-87; MALMO-10 ARG-292; MALMO-47
LYS-342; MALMO-5 GLN-400 AND MALMO-61 ALA-574.
PubMed=1518850; DOI=10.1073/pnas.89.17.8225;
Carlson J., Sakamoto Y., Laurell C.-B., Madison J., Watkins S.,
Putnam F.W.;
"Alloalbuminemia in Sweden: structural study and phenotypic
distribution of nine albumin variants.";
Proc. Natl. Acad. Sci. U.S.A. 89:8225-8229(1992).
[63]
VARIANT HERBORN GLU-264.
PubMed=8513793; DOI=10.1111/j.1432-1033.1993.tb17939.x;
Minchiotti L., Galliano M., Zapponi M.C., Tenni R.;
"The structural characterization and bilirubin-binding properties of
albumin Herborn, a [Lys240-->Glu] albumin mutant.";
Eur. J. Biochem. 214:437-444(1993).
[64]
VARIANT HAWKES BAY PHE-201.
PubMed=8347685; DOI=10.1016/0925-4439(93)90151-P;
Brennan S.O., Fellowes A.P.;
"Albumin Hawkes Bay; a low level variant caused by loss of a
sulphydryl group at position 177.";
Biochim. Biophys. Acta 1182:46-50(1993).
[65]
VARIANT ORTONOVO LYS-529.
PubMed=7902134; DOI=10.1016/0925-4439(93)90117-J;
Galliano M., Minchiotti L., Iadarola P., Stoppini M., Giagnoni P.,
Watkins S., Madison J., Putnam F.W.;
"Protein and DNA sequence analysis of a 'private' genetic variant:
albumin Ortonovo (Glu-505-->Lys).";
Biochim. Biophys. Acta 1225:27-32(1993).
[66]
VARIANTS LARINO TYR-27; TRADATE-2 GLN-249 AND CASERTA ASN-300.
PubMed=8022807; DOI=10.1073/pnas.91.14.6476;
Madison J., Galliano M., Watkins S., Minchiotti L., Porta F.,
Rossi A., Putnam F.W.;
"Genetic variants of human serum albumin in Italy: point mutants and a
carboxyl-terminal variant.";
Proc. Natl. Acad. Sci. U.S.A. 91:6476-6480(1994).
[67]
VARIANT FDAH HIS-242.
PubMed=8048949; DOI=10.1006/bbrc.1994.1998;
Sunthornthepvarakul T., Angkeow P., Weiss R.E., Hayashi Y.,
Retetoff S.;
"An identical missense mutation in the albumin gene results in
familial dysalbuminemic hyperthyroxinemia in 8 unrelated families.";
Biochem. Biophys. Res. Commun. 202:781-787(1994).
[68]
VARIANT FDAH HIS-242, AND PROTEIN SEQUENCE OF 25-51.
PubMed=7852505; DOI=10.1210/jcem.80.2.7852505;
Rushbrook J.I., Becker E., Schussler G.C., Divino C.M.;
"Identification of a human serum albumin species associated with
familial dysalbuminemic hyperthyroxinemia.";
J. Clin. Endocrinol. Metab. 80:461-467(1995).
[69]
VARIANT FDAH HIS-242.
PubMed=9329347; DOI=10.1210/jcem.82.10.4276;
Wada N., Chiba H., Shimizu C., Kijima H., Kubo M., Koike T.;
"A novel missense mutation in codon 218 of the albumin gene in a
distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a
Japanese kindred.";
J. Clin. Endocrinol. Metab. 82:3246-3250(1997).
[70]
VARIANT FDAH PRO-90.
PubMed=9589637; DOI=10.1210/jcem.83.5.4815;
Sunthornthepvarakul T., Likitmaskul S., Ngowngarmratana S.,
Angsusingha K., Kitvitayasak S., Scherberg N.H., Refetoff S.;
"Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly
inherited albumin defect.";
J. Clin. Endocrinol. Metab. 83:1448-1454(1998).
[71]
VARIANT TYR-73, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Urine;
PubMed=11680902;
DOI=10.1002/1615-9861(200101)1:1<93::AID-PROT93>3.0.CO;2-3;
Spahr C.S., Davis M.T., McGinley M.D., Robinson J.H., Bures E.J.,
Beierle J., Mort J., Courchesne P.L., Chen K., Wahl R.C., Yu W.,
Luethy R., Patterson S.D.;
"Towards defining the urinary proteome using liquid chromatography-
tandem mass spectrometry I. Profiling an unfractionated tryptic
digest.";
Proteomics 1:93-107(2001).
[72]
CHARACTERIZATION OF VARIANT KENITRA.
PubMed=11168369; DOI=10.1046/j.1432-1033.2001.01899.x;
Minchiotti L., Campagnoli M., Rossi A., Cosulich M.E., Monti M.,
Pucci P., Kragh-Hansen U., Granel B., Disdier P., Weiller P.J.,
Galliano M.;
"A nucleotide insertion and frameshift cause albumin Kenitra, an
extended and O-glycosylated mutant of human serum albumin with two
additional disulfide bridges.";
Eur. J. Biochem. 268:344-352(2001).
-!- FUNCTION: Serum albumin, the main protein of plasma, has a good
binding capacity for water, Ca(2+), Na(+), K(+), fatty acids,
hormones, bilirubin and drugs. Its main function is the regulation
of the colloidal osmotic pressure of blood. Major zinc transporter
in plasma, typically binds about 80% of all plasma zinc.
{ECO:0000269|PubMed:19021548}.
-!- INTERACTION:
Self; NbExp=8; IntAct=EBI-714423, EBI-714423;
P02786:TFRC; NbExp=2; IntAct=EBI-714423, EBI-355727;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P02768-1; Sequence=Displayed;
Name=2;
IsoId=P02768-2; Sequence=VSP_021275;
Name=3;
IsoId=P02768-3; Sequence=VSP_057389;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Plasma.
-!- PTM: Kenitra variant is partially O-glycosylated at Thr-620. It
has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-
606.
-!- PTM: Glycated in diabetic patients.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- PTM: Acetylated on Lys-223 by acetylsalicylic acid.
-!- POLYMORPHISM: A variant structure of albumin could lead to
increased binding of zinc resulting in an asymptomatic
augmentation of zinc concentration in the blood. The sequence
shown is that of variant albumin A.
-!- DISEASE: Hyperthyroxinemia, familial dysalbuminemic (FDAH)
[MIM:615999]: A disorder characterized by abnormally elevated
levels of total serum thyroxine (T4) in euthyroid patients. It is
due to abnormal serum albumin that binds T4 with enhanced
affinity. {ECO:0000269|PubMed:7852505, ECO:0000269|PubMed:8048949,
ECO:0000269|PubMed:9329347, ECO:0000269|PubMed:9589637}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Analbuminemia (ANALBA) [MIM:616000]: A rare autosomal
recessive disorder manifested by the presence of a very low amount
of circulating serum albumin. Affected individuals manifest mild
edema, hypotension, fatigue, and, occasionally, lower body
lipodystrophy (mainly in adult females). The most common
biochemical finding is hyperlipidemia, with a significant increase
in the total and LDL cholesterol concentrations, but normal
concentrations of HDL cholesterol and triglycerides.
{ECO:0000269|PubMed:8134387}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ALB/AFP/VDB family.
{ECO:0000255|PROSITE-ProRule:PRU00769}.
-!- CAUTION: A peptide arising from positions 166 to 174 was
originally (PubMed:3087352 and PubMed:2437111) termed neurotensin-
related peptide (NRP) or kinetensin and was thought to regulate
fat digestion, lipid absorption, and blood flow. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF22034.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAF69644.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAG35503.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Albumin Website;
URL="http://albumin.org";
-!- WEB RESOURCE: Name=Wikipedia; Note=Serum albumin entry;
URL="https://en.wikipedia.org/wiki/Serum_albumin";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/alb/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; V00494; CAA23753.1; -; mRNA.
EMBL; V00495; CAA23754.1; -; mRNA.
EMBL; M12523; AAA98797.1; -; Genomic_DNA.
EMBL; M12523; AAA98798.1; -; Genomic_DNA.
EMBL; AF190168; AAF01333.1; -; mRNA.
EMBL; AF542069; AAN17825.1; -; mRNA.
EMBL; A06977; CAA00606.1; -; mRNA.
EMBL; AY728024; AAU21642.1; -; mRNA.
EMBL; DQ986150; ABJ16448.1; -; mRNA.
EMBL; AY544124; AAT11155.1; -; mRNA.
EMBL; AY550967; AAT52213.1; -; mRNA.
EMBL; AF116645; AAF71067.1; -; mRNA.
EMBL; AF118090; AAF22034.1; ALT_INIT; mRNA.
EMBL; AF119840; AAF69594.1; -; mRNA.
EMBL; AF119890; AAF69644.1; ALT_INIT; mRNA.
EMBL; AF130077; AAG35503.1; ALT_INIT; mRNA.
EMBL; CR749331; CAH18185.1; -; mRNA.
EMBL; EF649953; ABS29264.1; -; Genomic_DNA.
EMBL; AC108157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX05676.1; -; Genomic_DNA.
EMBL; BC014308; AAH14308.1; -; mRNA.
EMBL; BC034023; AAH34023.1; -; mRNA.
EMBL; BC035969; AAH35969.1; -; mRNA.
EMBL; BC036003; AAH36003.1; -; mRNA.
EMBL; BC041789; AAH41789.1; -; mRNA.
EMBL; U22961; AAA64922.1; -; mRNA.
EMBL; AY358313; AAQ89947.1; -; mRNA.
EMBL; AH002596; AAA51688.1; -; Genomic_DNA.
CCDS; CCDS3555.1; -. [P02768-1]
PIR; A93743; ABHUS.
RefSeq; NP_000468.1; NM_000477.6. [P02768-1]
UniGene; Hs.418167; -.
UniGene; Hs.592379; -.
PDB; 1AO6; X-ray; 2.50 A; A/B=25-609.
PDB; 1BJ5; X-ray; 2.50 A; A=25-609.
PDB; 1BKE; X-ray; 3.15 A; A=28-608.
PDB; 1BM0; X-ray; 2.50 A; A/B=25-609.
PDB; 1E78; X-ray; 2.60 A; A/B=25-609.
PDB; 1E7A; X-ray; 2.20 A; A/B=25-609.
PDB; 1E7B; X-ray; 2.38 A; A/B=25-609.
PDB; 1E7C; X-ray; 2.40 A; A=25-609.
PDB; 1E7E; X-ray; 2.50 A; A=25-609.
PDB; 1E7F; X-ray; 2.43 A; A=25-609.
PDB; 1E7G; X-ray; 2.50 A; A=25-609.
PDB; 1E7H; X-ray; 2.43 A; A=25-609.
PDB; 1E7I; X-ray; 2.70 A; A=25-609.
PDB; 1GNI; X-ray; 2.40 A; A=25-609.
PDB; 1GNJ; X-ray; 2.60 A; A=25-609.
PDB; 1H9Z; X-ray; 2.50 A; A=25-609.
PDB; 1HA2; X-ray; 2.50 A; A=25-609.
PDB; 1HK1; X-ray; 2.65 A; A=25-609.
PDB; 1HK2; X-ray; 2.80 A; A=25-609.
PDB; 1HK3; X-ray; 2.80 A; A=25-609.
PDB; 1HK4; X-ray; 2.40 A; A=25-609.
PDB; 1HK5; X-ray; 2.70 A; A=25-609.
PDB; 1N5U; X-ray; 1.90 A; A=25-609.
PDB; 1O9X; X-ray; 3.20 A; A=25-609.
PDB; 1TF0; X-ray; 2.70 A; A=25-596.
PDB; 1UOR; X-ray; 2.80 A; A=25-609.
PDB; 1YSX; NMR; -; A=409-609.
PDB; 2BX8; X-ray; 2.70 A; A/B=25-609.
PDB; 2BXA; X-ray; 2.35 A; A/B=25-609.
PDB; 2BXB; X-ray; 3.20 A; A/B=25-609.
PDB; 2BXC; X-ray; 3.10 A; A/B=25-609.
PDB; 2BXD; X-ray; 3.05 A; A/B=25-609.
PDB; 2BXE; X-ray; 2.95 A; A/B=25-609.
PDB; 2BXF; X-ray; 2.95 A; A/B=25-609.
PDB; 2BXG; X-ray; 2.70 A; A/B=25-609.
PDB; 2BXH; X-ray; 2.25 A; A/B=25-609.
PDB; 2BXI; X-ray; 2.50 A; A=25-609.
PDB; 2BXK; X-ray; 2.40 A; A=25-609.
PDB; 2BXL; X-ray; 2.60 A; A=25-609.
PDB; 2BXM; X-ray; 2.50 A; A=25-609.
PDB; 2BXN; X-ray; 2.65 A; A=25-609.
PDB; 2BXO; X-ray; 2.60 A; A=25-609.
PDB; 2BXP; X-ray; 2.30 A; A=25-609.
PDB; 2BXQ; X-ray; 2.60 A; A=25-609.
PDB; 2ESG; X-ray; -; C=25-609.
PDB; 2I2Z; X-ray; 2.70 A; A=25-609.
PDB; 2I30; X-ray; 2.90 A; A=25-609.
PDB; 2N0X; NMR; -; A=432-447.
PDB; 2VDB; X-ray; 2.52 A; A=30-608.
PDB; 2VUE; X-ray; 2.42 A; A/B=25-609.
PDB; 2VUF; X-ray; 3.05 A; A/B=25-609.
PDB; 2XSI; X-ray; 2.70 A; A=25-609.
PDB; 2XVQ; X-ray; 2.90 A; A/B=25-609.
PDB; 2XVU; X-ray; 2.60 A; A/B=25-609.
PDB; 2XVV; X-ray; 2.40 A; A=25-609.
PDB; 2XVW; X-ray; 2.65 A; A=25-609.
PDB; 2XW0; X-ray; 2.40 A; A/B=25-609.
PDB; 2XW1; X-ray; 2.50 A; A/B=25-609.
PDB; 2YDF; X-ray; 2.75 A; A/B=25-609.
PDB; 3A73; X-ray; 2.19 A; A/B=25-609.
PDB; 3B9L; X-ray; 2.60 A; A=25-609.
PDB; 3B9M; X-ray; 2.70 A; A=25-609.
PDB; 3CX9; X-ray; 2.80 A; A=27-608.
PDB; 3JQZ; X-ray; 3.30 A; A/B=25-609.
PDB; 3JRY; X-ray; 2.30 A; A/B=25-609.
PDB; 3LU6; X-ray; 2.70 A; A/B=25-609.
PDB; 3LU7; X-ray; 2.80 A; A/B=25-609.
PDB; 3LU8; X-ray; 2.60 A; A/B=25-609.
PDB; 3SQJ; X-ray; 2.05 A; A/B=27-608.
PDB; 3TDL; X-ray; 2.60 A; A=25-609.
PDB; 3UIV; X-ray; 2.20 A; A/H=25-609.
PDB; 4BKE; X-ray; 2.35 A; A=1-609.
PDB; 4E99; X-ray; 2.30 A; A=25-609.
PDB; 4EMX; X-ray; 2.30 A; A/B=25-609.
PDB; 4G03; X-ray; 2.22 A; A/B=25-609.
PDB; 4G04; X-ray; 2.30 A; A/B=25-609.
PDB; 4HGK; X-ray; 3.04 A; A/B=25-609.
PDB; 4HGM; X-ray; 2.34 A; B=25-609.
PDB; 4IW1; X-ray; 2.56 A; A=25-609.
PDB; 4IW2; X-ray; 2.41 A; A=25-609.
PDB; 4K2C; X-ray; 3.23 A; A/B=25-609.
PDB; 4K71; X-ray; 2.40 A; A/D=25-609.
PDB; 4L8U; X-ray; 2.01 A; A=25-609.
PDB; 4L9K; X-ray; 2.40 A; A/B=25-609.
PDB; 4L9Q; X-ray; 2.70 A; A/B=25-609.
PDB; 4LA0; X-ray; 2.40 A; A/B=25-609.
PDB; 4LB2; X-ray; 2.80 A; A/B=25-609.
PDB; 4LB9; X-ray; 2.70 A; A=25-609.
PDB; 4N0F; X-ray; 3.02 A; D/G/J/M=25-609.
PDB; 4N0U; X-ray; 3.80 A; D=27-609.
PDB; 4S1Y; X-ray; 3.16 A; A=25-609.
PDB; 4Z69; X-ray; 2.19 A; A/I=25-609.
PDB; 5FUO; X-ray; 3.60 A; A=25-609.
PDB; 5ID7; X-ray; 2.26 A; A/B=25-609.
PDB; 5IFO; X-ray; 3.20 A; A=25-609.
PDB; 5IJF; X-ray; 2.65 A; A=25-609.
PDB; 5UJB; X-ray; 2.70 A; A/B=1-609.
PDB; 5X52; X-ray; 3.00 A; A/B=25-609.
PDBsum; 1AO6; -.
PDBsum; 1BJ5; -.
PDBsum; 1BKE; -.
PDBsum; 1BM0; -.
PDBsum; 1E78; -.
PDBsum; 1E7A; -.
PDBsum; 1E7B; -.
PDBsum; 1E7C; -.
PDBsum; 1E7E; -.
PDBsum; 1E7F; -.
PDBsum; 1E7G; -.
PDBsum; 1E7H; -.
PDBsum; 1E7I; -.
PDBsum; 1GNI; -.
PDBsum; 1GNJ; -.
PDBsum; 1H9Z; -.
PDBsum; 1HA2; -.
PDBsum; 1HK1; -.
PDBsum; 1HK2; -.
PDBsum; 1HK3; -.
PDBsum; 1HK4; -.
PDBsum; 1HK5; -.
PDBsum; 1N5U; -.
PDBsum; 1O9X; -.
PDBsum; 1TF0; -.
PDBsum; 1UOR; -.
PDBsum; 1YSX; -.
PDBsum; 2BX8; -.
PDBsum; 2BXA; -.
PDBsum; 2BXB; -.
PDBsum; 2BXC; -.
PDBsum; 2BXD; -.
PDBsum; 2BXE; -.
PDBsum; 2BXF; -.
PDBsum; 2BXG; -.
PDBsum; 2BXH; -.
PDBsum; 2BXI; -.
PDBsum; 2BXK; -.
PDBsum; 2BXL; -.
PDBsum; 2BXM; -.
PDBsum; 2BXN; -.
PDBsum; 2BXO; -.
PDBsum; 2BXP; -.
PDBsum; 2BXQ; -.
PDBsum; 2ESG; -.
PDBsum; 2I2Z; -.
PDBsum; 2I30; -.
PDBsum; 2N0X; -.
PDBsum; 2VDB; -.
PDBsum; 2VUE; -.
PDBsum; 2VUF; -.
PDBsum; 2XSI; -.
PDBsum; 2XVQ; -.
PDBsum; 2XVU; -.
PDBsum; 2XVV; -.
PDBsum; 2XVW; -.
PDBsum; 2XW0; -.
PDBsum; 2XW1; -.
PDBsum; 2YDF; -.
PDBsum; 3A73; -.
PDBsum; 3B9L; -.
PDBsum; 3B9M; -.
PDBsum; 3CX9; -.
PDBsum; 3JQZ; -.
PDBsum; 3JRY; -.
PDBsum; 3LU6; -.
PDBsum; 3LU7; -.
PDBsum; 3LU8; -.
PDBsum; 3SQJ; -.
PDBsum; 3TDL; -.
PDBsum; 3UIV; -.
PDBsum; 4BKE; -.
PDBsum; 4E99; -.
PDBsum; 4EMX; -.
PDBsum; 4G03; -.
PDBsum; 4G04; -.
PDBsum; 4HGK; -.
PDBsum; 4HGM; -.
PDBsum; 4IW1; -.
PDBsum; 4IW2; -.
PDBsum; 4K2C; -.
PDBsum; 4K71; -.
PDBsum; 4L8U; -.
PDBsum; 4L9K; -.
PDBsum; 4L9Q; -.
PDBsum; 4LA0; -.
PDBsum; 4LB2; -.
PDBsum; 4LB9; -.
PDBsum; 4N0F; -.
PDBsum; 4N0U; -.
PDBsum; 4S1Y; -.
PDBsum; 4Z69; -.
PDBsum; 5FUO; -.
PDBsum; 5ID7; -.
PDBsum; 5IFO; -.
PDBsum; 5IJF; -.
PDBsum; 5UJB; -.
PDBsum; 5X52; -.
ProteinModelPortal; P02768; -.
SMR; P02768; -.
BioGrid; 106715; 190.
DIP; DIP-29902N; -.
IntAct; P02768; 171.
MINT; MINT-3004222; -.
STRING; 9606.ENSP00000295897; -.
BindingDB; P02768; -.
ChEMBL; CHEMBL3253; -.
DrugBank; DB07517; 3-CARBOXY-4-METHYL-5-PROPYL-2-FURANPROPIONIC.
DrugBank; DB07992; 3-SULFOOXY-1H-INDOLE.
DrugBank; DB05812; Abiraterone.
DrugBank; DB01418; Acenocoumarol.
DrugBank; DB01614; Acepromazine.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00459; Acitretin.
DrugBank; DB00802; Alfentanil.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB00415; Ampicillin.
DrugBank; DB04557; Arachidonic Acid.
DrugBank; DB00995; Auranofin.
DrugBank; DB07402; Azapropazone.
DrugBank; DB01294; Bismuth Subsalicylate.
DrugBank; DB08907; Canagliflozin.
DrugBank; DB01197; Captopril.
DrugBank; DB00456; Cefalotin.
DrugBank; DB01327; Cefazolin.
DrugBank; DB00274; Cefmetazole.
DrugBank; DB01328; Cefonicid.
DrugBank; DB01329; Cefoperazone.
DrugBank; DB00493; Cefotaxime.
DrugBank; DB01330; Cefotetan.
DrugBank; DB00430; Cefpiramide.
DrugBank; DB01212; Ceftriaxone.
DrugBank; DB00482; Celecoxib.
DrugBank; DB00567; Cephalexin.
DrugBank; DB00477; Chlorpromazine.
DrugBank; DB01242; Clomipramine.
DrugBank; DB01068; Clonazepam.
DrugBank; DB01147; Cloxacillin.
DrugBank; DB03600; Decanoic Acid.
DrugBank; DB01189; Desflurane.
DrugBank; DB00829; Diazepam.
DrugBank; DB00586; Diclofenac.
DrugBank; DB00861; Diflunisal.
DrugBank; DB01396; Digitoxin.
DrugBank; DB04855; Dronedarone.
DrugBank; DB00228; Enflurane.
DrugBank; DB08899; Enzalutamide.
DrugBank; DB00530; Erlotinib.
DrugBank; DB00199; Erythromycin.
DrugBank; DB00783; Estradiol.
DrugBank; DB00655; Estrone.
DrugBank; DB04574; Estrone sulfate.
DrugBank; DB00903; Etacrynic acid.
DrugBank; DB00749; Etodolac.
DrugBank; DB00573; Fenoprofen.
DrugBank; DB00544; Fluorouracil.
DrugBank; DB00472; Fluoxetine.
DrugBank; DB00712; Flurbiprofen.
DrugBank; DB01320; Fosphenytoin.
DrugBank; DB06716; Fospropofol.
DrugBank; DB00695; Furosemide.
DrugBank; DB00743; Gadobenic acid.
DrugBank; DB06705; Gadofosveset trisodium.
DrugBank; DB01044; Gatifloxacin.
DrugBank; DB00317; Gefitinib.
DrugBank; DB01120; Gliclazide.
DrugBank; DB01016; Glyburide.
DrugBank; DB01159; Halothane.
DrugBank; DB00070; Hyaluronidase.
DrugBank; DB06205; Hyaluronidase (Human Recombinant).
DrugBank; DB01050; Ibuprofen.
DrugBank; DB00619; Imatinib.
DrugBank; DB00328; Indomethacin.
DrugBank; DB01307; Insulin Detemir.
DrugBank; DB04711; Iodipamide.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00753; Isoflurane.
DrugBank; DB08820; Ivacaftor.
DrugBank; DB01587; Ketazolam.
DrugBank; DB01009; Ketoprofen.
DrugBank; DB03017; Lauric Acid.
DrugBank; DB00451; Levothyroxine.
DrugBank; DB00279; Liothyronine.
DrugBank; DB01583; Liotrix.
DrugBank; DB00678; Losartan.
DrugBank; DB09280; Lumacaftor.
DrugBank; DB08932; Macitentan.
DrugBank; DB01397; Magnesium salicylate.
DrugBank; DB00931; Methacycline.
DrugBank; DB00563; Methotrexate.
DrugBank; DB06710; Methyltestosterone.
DrugBank; DB08893; Mirabegron.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB01183; Naloxone.
DrugBank; DB00788; Naproxen.
DrugBank; DB00731; Nateglinide.
DrugBank; DB00717; Norethisterone.
DrugBank; DB00540; Nortriptyline.
DrugBank; DB00334; Olanzapine.
DrugBank; DB04224; Oleic Acid.
DrugBank; DB00776; Oxcarbazepine.
DrugBank; DB06412; Oxymetholone.
DrugBank; DB03585; Oxyphenbutazone.
DrugBank; DB03796; Palmitic Acid.
DrugBank; DB00454; Pethidine.
DrugBank; DB00946; Phenprocoumon.
DrugBank; DB00252; Phenytoin.
DrugBank; DB01621; Pipotiazine.
DrugBank; DB00554; Piroxicam.
DrugBank; DB08860; Pitavastatin.
DrugBank; DB06209; Prasugrel.
DrugBank; DB00635; Prednisone.
DrugBank; DB01032; Probenecid.
DrugBank; DB00818; Propofol.
DrugBank; DB00912; Repaglinide.
DrugBank; DB01045; Rifampicin.
DrugBank; DB08931; Riociguat.
DrugBank; DB00412; Rosiglitazone.
DrugBank; DB01098; Rosuvastatin.
DrugBank; DB06201; Rufinamide.
DrugBank; DB00936; Salicylic acid.
DrugBank; DB01232; Saquinavir.
DrugBank; DB01236; Sevoflurane.
DrugBank; DB06290; Simeprevir.
DrugBank; DB00815; Sodium lauryl sulfate.
DrugBank; DB03193; Stearic acid.
DrugBank; DB00364; Sucralfate.
DrugBank; DB01581; Sulfamerazine.
DrugBank; DB01582; Sulfamethazine.
DrugBank; DB00576; Sulfamethizole.
DrugBank; DB01015; Sulfamethoxazole.
DrugBank; DB00605; Sulindac.
DrugBank; DB00864; Tacrolimus.
DrugBank; DB05521; Telaprevir.
DrugBank; DB00624; Testosterone.
DrugBank; DB00759; Tetracycline.
DrugBank; DB01622; Thioproperazine.
DrugBank; DB01623; Thiothixene.
DrugBank; DB01056; Tocainide.
DrugBank; DB08895; Tofacitinib.
DrugBank; DB08867; Ulipristal.
DrugBank; DB00177; Valsartan.
DrugBank; DB00512; Vancomycin.
DrugBank; DB05294; Vandetanib.
DrugBank; DB08881; Vemurafenib.
DrugBank; DB08828; Vismodegib.
DrugBank; DB00682; Warfarin.
DrugBank; DB00137; Xanthophyll.
DrugBank; DB00495; Zidovudine.
Allergome; 763; Hom s HSA.
iPTMnet; P02768; -.
PhosphoSitePlus; P02768; -.
SwissPalm; P02768; -.
UniCarbKB; P02768; -.
BioMuta; ALB; -.
DMDM; 113576; -.
DOSAC-COBS-2DPAGE; P02768; -.
OGP; P02768; -.
REPRODUCTION-2DPAGE; IPI00384697; -.
REPRODUCTION-2DPAGE; IPI00745872; -.
REPRODUCTION-2DPAGE; P02768; -.
SWISS-2DPAGE; P02768; -.
UCD-2DPAGE; P02768; -.
PaxDb; P02768; -.
PeptideAtlas; P02768; -.
PRIDE; P02768; -.
DNASU; 213; -.
Ensembl; ENST00000295897; ENSP00000295897; ENSG00000163631. [P02768-1]
Ensembl; ENST00000621085; ENSP00000483421; ENSG00000163631. [P02768-3]
GeneID; 213; -.
KEGG; hsa:213; -.
UCSC; uc003hgs.5; human. [P02768-1]
UCSC; uc062xfr.1; human.
CTD; 213; -.
DisGeNET; 213; -.
GeneCards; ALB; -.
HGNC; HGNC:399; ALB.
HPA; CAB006262; -.
HPA; HPA031024; -.
HPA; HPA031025; -.
MalaCards; ALB; -.
MIM; 103600; gene.
MIM; 615999; phenotype.
MIM; 616000; phenotype.
neXtProt; NX_P02768; -.
OpenTargets; ENSG00000163631; -.
Orphanet; 86816; Congenital analbuminemia.
Orphanet; 276271; Familial dysalbuminemic hyperthyroxinemia.
PharmGKB; PA24690; -.
eggNOG; ENOG410IIRZ; Eukaryota.
eggNOG; ENOG410Z40H; LUCA.
GeneTree; ENSGT00390000000113; -.
HOGENOM; HOG000293137; -.
HOVERGEN; HBG004207; -.
InParanoid; P02768; -.
KO; K16141; -.
OMA; KTCVADE; -.
OrthoDB; EOG091G0F5F; -.
PhylomeDB; P02768; -.
TreeFam; TF335561; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-159418; Recycling of bile acids and salts.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5619058; Defective SLCO1B3 causes hyperbilirubinemia, Rotor type (HBLRR).
Reactome; R-HSA-5619110; Defective SLCO1B1 causes hyperbilirubinemia, Rotor type (HBLRR).
Reactome; R-HSA-879518; Transport of organic anions.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-8964058; HDL remodeling.
SIGNOR; P02768; -.
ChiTaRS; ALB; human.
EvolutionaryTrace; P02768; -.
GeneWiki; Serum_albumin; -.
GenomeRNAi; 213; -.
PMAP-CutDB; P02768; -.
PRO; PR:P02768; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163631; -.
ExpressionAtlas; P02768; baseline and differential.
Genevisible; P02768; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0016209; F:antioxidant activity; NAS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0005507; F:copper ion binding; NAS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB.
GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IDA:UniProtKB.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; TAS:Reactome.
GO; GO:0051659; P:maintenance of mitochondrion location; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043069; P:negative regulation of programmed cell death; NAS:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0001895; P:retina homeostasis; IEP:UniProtKB.
GO; GO:0043252; P:sodium-independent organic anion transport; TAS:Reactome.
GO; GO:0006810; P:transport; TAS:UniProtKB.
CDD; cd00015; ALBUMIN; 3.
InterPro; IPR000264; ALB/AFP/VDB.
InterPro; IPR020858; Serum_albumin-like.
InterPro; IPR021177; Serum_albumin/AFP/Afamin.
InterPro; IPR020857; Serum_albumin_CS.
InterPro; IPR014760; Serum_albumin_N.
PANTHER; PTHR11385; PTHR11385; 1.
Pfam; PF00273; Serum_albumin; 3.
PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
PRINTS; PR00802; SERUMALBUMIN.
SMART; SM00103; ALBUMIN; 3.
SUPFAM; SSF48552; SSF48552; 3.
PROSITE; PS00212; ALBUMIN_1; 3.
PROSITE; PS51438; ALBUMIN_2; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing;
Cleavage on pair of basic residues; Complete proteome; Copper;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycation; Glycoprotein; Lipid-binding; Metal-binding; Methylation;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Signal; Zinc.
SIGNAL 1 18
PROPEP 19 24
/FTId=PRO_0000001067.
CHAIN 25 609 Serum albumin.
/FTId=PRO_0000001068.
DOMAIN 19 210 Albumin 1. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 211 403 Albumin 2. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
DOMAIN 404 601 Albumin 3. {ECO:0000255|PROSITE-
ProRule:PRU00769}.
METAL 27 27 Copper. {ECO:0000250}.
METAL 91 91 Zinc.
METAL 123 123 Zinc.
METAL 271 271 Zinc.
METAL 273 273 Zinc.
BINDING 264 264 Bilirubin.
SITE 28 28 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 44 44 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 65 65 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 88 88 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 97 97 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 117 117 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 130 130 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 160 160 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 183 183 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 198 198 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 205 205 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 214 214 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 219 219 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 223 223 Aspirin-acetylated lysine.
SITE 229 229 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 236 236 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 264 264 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 286 286 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 298 298 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 310 310 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 383 383 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 396 396 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 413 413 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 426 426 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 438 438 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 456 456 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 460 460 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 490 490 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 499 499 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 524 524 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 543 543 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 548 548 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 562 562 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 565 565 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 581 581 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 584 584 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 588 588 Not glycated.
{ECO:0000269|PubMed:15047055}.
SITE 598 598 Not glycated.
{ECO:0000269|PubMed:15047055}.
MOD_RES 29 29 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 82 82 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
MOD_RES 89 89 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
MOD_RES 107 107 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 229 229 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 444 444 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 460 460 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 543 543 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
MOD_RES 558 558 N6-methyllysine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 588 588 N6-succinyllysine.
{ECO:0000250|UniProtKB:P07724}.
CARBOHYD 36 36 N-linked (Glc) (glycation) lysine.
{ECO:0000305}.
CARBOHYD 75 75 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 161 161 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 186 186 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 223 223 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 249 249 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 257 257 N-linked (Glc) (glycation) lysine.
{ECO:0000305}.
CARBOHYD 300 300 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 305 305 N-linked (Glc) (glycation) lysine.
CARBOHYD 337 337 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 341 341 N-linked (Glc) (glycation) lysine.
{ECO:0000305}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine; in
variant Redhill.
/FTId=CAR_000226.
CARBOHYD 347 347 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 375 375 N-linked (Glc) (glycation) lysine.
{ECO:0000305}.
CARBOHYD 402 402 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 437 437 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 463 463 N-linked (Glc) (glycation) lysine.
CARBOHYD 468 468 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine; in
variant Casebrook.
/FTId=CAR_000069.
CARBOHYD 549 549 N-linked (Glc) (glycation) lysine.
CARBOHYD 558 558 N-linked (Glc) (glycation) lysine;
alternate. {ECO:0000305}.
CARBOHYD 560 560 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 569 569 N-linked (Glc) (glycation) lysine; in
vitro.
CARBOHYD 597 597 N-linked (Glc) (glycation) lysine; in
vitro.
DISULFID 77 86 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 99 115 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 114 125 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 148 193 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 192 201 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 224 270 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 269 277 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 289 303 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 302 313 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 340 385 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 384 393 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 416 462 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 461 472 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 485 501 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 500 511 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 538 583 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
DISULFID 582 591 {ECO:0000255|PROSITE-ProRule:PRU00769,
ECO:0000269|Ref.28}.
VAR_SEQ 43 234 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.9}.
/FTId=VSP_021275.
VAR_SEQ 164 376 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057389.
VARIANT 23 23 R -> C (in Redhill/Malmo-I/Tradate;
associated with T-344 in Redhill;
dbSNP:rs80008208).
{ECO:0000269|PubMed:1518850}.
/FTId=VAR_000499.
VARIANT 23 23 R -> H (in Fukuoka-2/Lille/Taipei/Varese/
Komagome-3; dbSNP:rs72552709).
{ECO:0000269|PubMed:1946412,
ECO:0000269|PubMed:2247440,
ECO:0000269|PubMed:2911589}.
/FTId=VAR_000500.
VARIANT 24 24 R -> L (in Jaffna; dbSNP:rs74821926).
/FTId=VAR_000501.
VARIANT 24 24 R -> P (in Takefu/Honolulu-1;
dbSNP:rs74821926).
{ECO:0000269|PubMed:2404284}.
/FTId=VAR_000502.
VARIANT 24 24 R -> Q (in Christchurch/Honolulu-2;
dbSNP:rs74821926).
{ECO:0000269|PubMed:2404284,
ECO:0000269|PubMed:2762316,
ECO:0000269|PubMed:2911589}.
/FTId=VAR_000503.
VARIANT 25 25 D -> V (in Bleinheim/Iowa city-2;
dbSNP:rs75353611).
{ECO:0000269|PubMed:1946412}.
/FTId=VAR_000504.
VARIANT 27 27 H -> Q (in Nagasaki-3; dbSNP:rs76285851).
/FTId=VAR_000505.
VARIANT 27 27 H -> Y (in Larino; dbSNP:rs141733599).
{ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:8022807}.
/FTId=VAR_000506.
VARIANT 73 73 F -> Y. {ECO:0000269|PubMed:11680902}.
/FTId=VAR_010657.
VARIANT 84 84 E -> K (in Torino; dbSNP:rs77050410).
{ECO:0000269|PubMed:2247440}.
/FTId=VAR_000507.
VARIANT 87 87 D -> N (in Malmo-95/Dalakarlia;
dbSNP:rs78574148).
{ECO:0000269|PubMed:1518850}.
/FTId=VAR_000508.
VARIANT 90 90 L -> P (in FDAH; dbSNP:rs77892378).
{ECO:0000269|PubMed:9589637}.
/FTId=VAR_013011.
VARIANT 106 106 E -> K (in Vibo Valentia;
dbSNP:rs80296402).
{ECO:0000269|PubMed:2247440}.
/FTId=VAR_000509.
VARIANT 121 121 E -> G. {ECO:0000269|PubMed:6275391}.
/FTId=VAR_014290.
VARIANT 138 138 R -> G (in Yanomama-2; dbSNP:rs77238412).
/FTId=VAR_000510.
VARIANT 143 143 E -> K (in Nagoya; dbSNP:rs75522063).
{ECO:0000269|PubMed:2404284}.
/FTId=VAR_000511.
VARIANT 146 146 V -> E (in Tregasio; dbSNP:rs77752336).
/FTId=VAR_013012.
VARIANT 152 152 H -> R (in Komagome-2; dbSNP:rs80095457).
{ECO:0000269|PubMed:1946412}.
/FTId=VAR_000512.
VARIANT 201 201 C -> F (in Hawkes bay; dbSNP:rs77656691).
{ECO:0000269|PubMed:8347685}.
/FTId=VAR_000513.
VARIANT 215 215 A -> T (in dbSNP:rs3210154).
/FTId=VAR_014291.
VARIANT 215 215 A -> V (in dbSNP:rs3204504).
/FTId=VAR_014292.
VARIANT 220 220 Q -> L (in dbSNP:rs3210163).
/FTId=VAR_014293.
VARIANT 242 242 R -> H (in FDAH; dbSNP:rs75002628).
{ECO:0000269|PubMed:7852505,
ECO:0000269|PubMed:8048949,
ECO:0000269|PubMed:9329347}.
/FTId=VAR_000514.
VARIANT 242 242 R -> P (in FDAH; dbSNP:rs75002628).
/FTId=VAR_013013.
VARIANT 249 249 K -> Q (in Tradate-2; dbSNP:rs79804069).
{ECO:0000269|PubMed:8022807}.
/FTId=VAR_000515.
VARIANT 264 264 K -> E (in Herborn; dbSNP:rs79377490).
{ECO:0000269|PubMed:8513793}.
/FTId=VAR_000516.
VARIANT 292 292 Q -> R (in Malmo-10; dbSNP:rs80002911).
{ECO:0000269|PubMed:1518850}.
/FTId=VAR_000517.
VARIANT 293 293 D -> G (in Nagasaki-1; dbSNP:rs79744198).
{ECO:0000269|PubMed:2762316}.
/FTId=VAR_000518.
VARIANT 300 300 K -> N (in Caserta; dbSNP:rs74718349).
{ECO:0000269|PubMed:8022807}.
/FTId=VAR_000519.
VARIANT 337 337 K -> N (in Canterbury/New Guinea/
Tagliacozzo/Cuneo/Cooperstown;
dbSNP:rs72552710).
{ECO:0000269|PubMed:2404284,
ECO:0000269|PubMed:2911589,
ECO:0000269|PubMed:3828358}.
/FTId=VAR_000520.
VARIANT 338 338 D -> G (in Bergamo; dbSNP:rs76242087).
/FTId=VAR_013014.
VARIANT 338 338 D -> V (in Brest; dbSNP:rs76242087).
/FTId=VAR_013015.
VARIANT 342 342 N -> K (in Malmo-47; dbSNP:rs77544362).
{ECO:0000269|PubMed:1518850}.
/FTId=VAR_000521.
VARIANT 344 344 A -> T (in Redhill; associated with C-23;
dbSNP:rs78953271).
/FTId=VAR_000522.
VARIANT 345 345 E -> K (in Roma; dbSNP:rs72552711).
/FTId=VAR_000523.
VARIANT 357 357 E -> K (in Sondrio; dbSNP:rs77354753).
{ECO:0000269|PubMed:1347703}.
/FTId=VAR_000524.
VARIANT 378 378 E -> K (in Hiroshima-1;
dbSNP:rs76593094).
{ECO:0000269|PubMed:2762316,
ECO:0000269|Ref.5}.
/FTId=VAR_000525.
VARIANT 382 382 E -> K (in Coari I/Porto Alegre;
dbSNP:rs75791663).
/FTId=VAR_000526.
VARIANT 383 383 K -> N (in Trieste; dbSNP:rs75069738).
/FTId=VAR_013016.
VARIANT 389 389 D -> H (in Parklands; dbSNP:rs77187142).
/FTId=VAR_000527.
VARIANT 389 389 D -> V (in Iowa city-1;
dbSNP:rs78538497).
{ECO:0000269|PubMed:1946412}.
/FTId=VAR_000528.
VARIANT 396 396 K -> E (in Naskapi/Mersin/Komagome-1;
dbSNP:rs78166690).
{ECO:0000269|PubMed:1946412,
ECO:0000269|PubMed:3474609,
ECO:0000269|PubMed:3479777}.
/FTId=VAR_000529.
VARIANT 399 399 D -> N (in Nagasaki-2; dbSNP:rs77514449).
{ECO:0000269|PubMed:3479777}.
/FTId=VAR_000530.
VARIANT 400 400 E -> K (in Tochigi; dbSNP:rs79047363).
{ECO:0000269|PubMed:2762316}.
/FTId=VAR_000531.
VARIANT 400 400 E -> Q (in Malmo-5; dbSNP:rs79047363).
{ECO:0000269|PubMed:1518850}.
/FTId=VAR_000532.
VARIANT 406 406 E -> K (in Hiroshima-2;
dbSNP:rs76483862).
{ECO:0000269|PubMed:2762316}.
/FTId=VAR_000533.
VARIANT 420 420 E -> K. {ECO:0000269|PubMed:6171778}.
/FTId=VAR_014294.
VARIANT 434 434 R -> C (in Liprizzi; dbSNP:rs78575701).
/FTId=VAR_013017.
VARIANT 490 490 K -> E (in dbSNP:rs1063469).
/FTId=VAR_014295.
VARIANT 503 503 E -> K (in Dublin; dbSNP:rs80259813).
/FTId=VAR_000534.
VARIANT 518 518 D -> N (in Casebrook; dbSNP:rs75920790).
{ECO:0000269|PubMed:1859851}.
/FTId=VAR_000535.
VARIANT 525 525 E -> K (in Manaus-1/Adana/Lambadi/
Vancouver; dbSNP:rs75523493).
{ECO:0000269|PubMed:2404284}.
/FTId=VAR_000536.
VARIANT 529 529 E -> K (in Ortonovo; dbSNP:rs74826639).
{ECO:0000269|PubMed:7902134}.
/FTId=VAR_000537.
VARIANT 557 557 V -> M (in Maddaloni; dbSNP:rs78284052).
/FTId=VAR_013018.
VARIANT 560 560 K -> E (in Castel di Sangro;
dbSNP:rs77645174).
/FTId=VAR_000538.
VARIANT 565 565 K -> E (in Maku; dbSNP:rs80345158).
{ECO:0000269|PubMed:3479777}.
/FTId=VAR_000539.
VARIANT 574 574 D -> A (in Malmo-61; dbSNP:rs79738788).
{ECO:0000269|PubMed:1518850}.
/FTId=VAR_000541.
VARIANT 574 574 D -> G (in Mexico; dbSNP:rs79738788).
{ECO:0000269|PubMed:3474609}.
/FTId=VAR_000540.
VARIANT 584 584 K -> E (in Church bay; dbSNP:rs76671808).
/FTId=VAR_013019.
VARIANT 587 587 D -> N (in Fukuoka-1/Paris-2;
dbSNP:rs76587671).
{ECO:0000269|PubMed:1347703,
ECO:0000269|PubMed:2404284}.
/FTId=VAR_000542.
VARIANT 589 589 E -> K (in Osaka-1; dbSNP:rs75709682).
{ECO:0000269|PubMed:2404284}.
/FTId=VAR_000543.
VARIANT 594 594 E -> K (in Osaka-2/Phnom Phen/albumin B/
Verona; dbSNP:rs79228041).
{ECO:0000269|PubMed:2404284,
ECO:0000269|PubMed:2762316,
ECO:0000269|PubMed:2911589}.
/FTId=VAR_000544.
VARIANT 596 609 GKKLVAASQAALGL -> PTMRIRERK (in Venezia).
/FTId=VAR_000547.
VARIANT 597 597 K -> E (in Gent/Milano Fast;
dbSNP:rs80106970).
/FTId=VAR_000545.
VARIANT 598 598 K -> N (in Vanves; dbSNP:rs75738598).
/FTId=VAR_000546.
VARIANT 599 609 LVAASQAALGL -> TCCCKSSCLRLITSHLKASQPTMRIR
ERK (in Kenitra).
/FTId=VAR_012981.
CONFLICT 55 55 L -> P (in Ref. 11; CAH18185).
{ECO:0000305}.
CONFLICT 122 122 R -> S (in Ref. 4; AAF01333).
{ECO:0000305}.
CONFLICT 155 155 E -> Q (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 174 174 Y -> L (in Ref. 24; AA sequence and 25;
AA sequence). {ECO:0000305}.
CONFLICT 194 194 Q -> E (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 327 332 PSLAAD -> MFVLLC (in Ref. 10; AAF71067).
{ECO:0000305}.
CONFLICT 405 405 V -> A (in Ref. 10; AAF71067).
{ECO:0000305}.
CONFLICT 409 409 Q -> E (in Ref. 15; AAH14308).
{ECO:0000305}.
CONFLICT 441 441 Q -> E (in Ref. 2; CAA23753).
{ECO:0000305}.
CONFLICT 466 466 E -> G (in Ref. 4; AAF01333).
{ECO:0000305}.
CONFLICT 488 489 HE -> EH (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 490 490 K -> R (in Ref. 11; CAH18185).
{ECO:0000305}.
CONFLICT 525 525 E -> Q (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 551 551 T -> A (in Ref. 11; CAH18185).
{ECO:0000305}.
CONFLICT 560 560 K -> R (in Ref. 11; CAH18185).
{ECO:0000305}.
CONFLICT 604 604 Q -> R (in Ref. 5; AAN17825).
{ECO:0000305}.
HELIX 30 38 {ECO:0000244|PDB:1N5U}.
HELIX 40 54 {ECO:0000244|PDB:1N5U}.
STRAND 55 58 {ECO:0000244|PDB:2BXH}.
HELIX 60 79 {ECO:0000244|PDB:1N5U}.
TURN 84 87 {ECO:0000244|PDB:1N5U}.
HELIX 90 99 {ECO:0000244|PDB:1N5U}.
TURN 101 103 {ECO:0000244|PDB:2BXH}.
HELIX 104 108 {ECO:0000244|PDB:1N5U}.
HELIX 109 116 {ECO:0000244|PDB:1N5U}.
HELIX 119 128 {ECO:0000244|PDB:1N5U}.
STRAND 130 132 {ECO:0000244|PDB:4N0F}.
HELIX 144 153 {ECO:0000244|PDB:1N5U}.
HELIX 155 169 {ECO:0000244|PDB:1N5U}.
STRAND 171 173 {ECO:0000244|PDB:5ID7}.
HELIX 175 192 {ECO:0000244|PDB:1N5U}.
STRAND 195 197 {ECO:0000244|PDB:4L8U}.
HELIX 198 230 {ECO:0000244|PDB:1N5U}.
HELIX 232 246 {ECO:0000244|PDB:1N5U}.
STRAND 248 250 {ECO:0000244|PDB:1BJ5}.
HELIX 252 271 {ECO:0000244|PDB:1N5U}.
HELIX 274 289 {ECO:0000244|PDB:1N5U}.
HELIX 290 294 {ECO:0000244|PDB:1N5U}.
HELIX 297 299 {ECO:0000244|PDB:4Z69}.
HELIX 300 303 {ECO:0000244|PDB:1N5U}.
HELIX 307 315 {ECO:0000244|PDB:1N5U}.
HELIX 330 333 {ECO:0000244|PDB:1N5U}.
STRAND 336 338 {ECO:0000244|PDB:2BXP}.
HELIX 339 345 {ECO:0000244|PDB:1N5U}.
HELIX 347 360 {ECO:0000244|PDB:1N5U}.
STRAND 363 365 {ECO:0000244|PDB:4N0F}.
HELIX 367 384 {ECO:0000244|PDB:1N5U}.
STRAND 387 389 {ECO:0000244|PDB:1N5U}.
HELIX 390 394 {ECO:0000244|PDB:1N5U}.
HELIX 397 422 {ECO:0000244|PDB:1N5U}.
HELIX 424 438 {ECO:0000244|PDB:1N5U}.
STRAND 440 442 {ECO:0000244|PDB:2BXC}.
HELIX 444 461 {ECO:0000244|PDB:1N5U}.
STRAND 462 464 {ECO:0000244|PDB:2BXH}.
HELIX 466 488 {ECO:0000244|PDB:1N5U}.
STRAND 489 491 {ECO:0000244|PDB:4G03}.
HELIX 495 502 {ECO:0000244|PDB:1N5U}.
TURN 505 507 {ECO:0000244|PDB:1N5U}.
HELIX 508 513 {ECO:0000244|PDB:1N5U}.
STRAND 519 521 {ECO:0000244|PDB:4E99}.
HELIX 529 531 {ECO:0000244|PDB:1N5U}.
HELIX 535 538 {ECO:0000244|PDB:1N5U}.
HELIX 542 559 {ECO:0000244|PDB:1N5U}.
STRAND 561 563 {ECO:0000244|PDB:1E7A}.
HELIX 565 583 {ECO:0000244|PDB:1N5U}.
STRAND 584 587 {ECO:0000244|PDB:1N5U}.
HELIX 588 590 {ECO:0000244|PDB:2BXG}.
TURN 591 593 {ECO:0000244|PDB:1N5U}.
HELIX 594 606 {ECO:0000244|PDB:1N5U}.
SEQUENCE 609 AA; 69367 MW; F88FF61DD242E818 CRC64;
MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF
EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP
ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF
FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV
ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK
ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR
RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE
QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV
LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL
SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV
AASQAALGL


Related products :

Catalog number Product name Quantity
orb81168 Human Serum Albumin protein Human Serum Albumin contains 584 amino acid residues derived from the prototypical human serum albumin sequence. Suitable for use in biochemical, excipient (an inert substa 100 mg
700-300-10 Albumin-X, Albumin (multiple species) removal kit (sufficient to remove 2-3 mg albumin or process ~50-100 ul serum; 10 mini-columns ~250 ul resin) 1 kit
700-1250-10 Albumin-X, Albumin (multiple species) removal kit (sufficient to remove 6-10 mg albumin or process ~200-300 ul serum; 10 mini-columns ~1.25 ml resin) 1 kit
700-300-10 Albumin-X, Albumin (multiple species) removal kit (sufficient to remove 2-3 mg albumin or process ~50-100 ul serum; 10 mini-columns ~250 ul resin) Species Reactivity: 1 kit Product tipe: Kit
700-1250-10 Albumin-X, Albumin (multiple species) removal kit (sufficient to remove 6-10 mg albumin or process ~200-300 ul serum; 10 mini-columns ~1.25 ml resin) Species Reactivity: 1 kit Product tipe: Kit
orb80232 Rat Serum Albumin Chromatographically purified rat albumin. Purified rat albumin may be used as a reference antigen, calibrator, coating protein and blocking agent in a variety of immunoassays includi 10 mg
LT-700MS-300ULX-10XC Albumin-X, Albumin (multiple species) removal kit (sufficient to remove 6-10 mg albumin or process ~200-300 ul serum; 10 mini-columns ~1.25 ml resin) Species Reactivity: 1 kit Product tipe: Kit
orb80191 Bovine Serum Albumin Fr.V Tetramethylrhodamine isothiocyanate-conjugated bovine serum albumin, Cohn fraction V. As an efficient counterstain for cell an tissue substrates with immunoconjugates with a 1 ml
orb80213 Monkey Serum Albumin Chromatographically purified monkey albumin. Confirmed and tested by immunoelectrophoresis and double radial immunodiffusion (Ouchterlony) using antisera to total serum proteins, 10 mg
orb80190 Bovine Serum Albumin Fr.V Fluorescein isothiocyanate-conjugated bovine serum albumin, Cohn fraction V. As an efficient counterstain for cell an tissue substrates with immunoconjugates with a label con 10 mg
AK8972 Human Serum Albumin- Caprylate Reduced, Protease Free Powder (Diagnostic Grade) Human Serum Albumin Inquire
orb80972 Bovine Serum Albumin protein Contains 583 amino acid residues derived from the prototypical bovine serum albumin sequence. Suitable for use as biochemical, excipient (an inert substance used as diluen 10 g
orb81320 Human Serum Albumin protein Recombinant Human Serum Albumin produced in yeast is a single, non-glycosylated, polypeptide chain containing 585 amino acids and having a molecular mass of 66441 Dalton.Th 10 mg
AK8970 Human Serum Albumin-Fatty Acid Free (Diagnostic Grade) Human Serum Albumin Inquire
LF-MA41360 anti-Serum Albumin (AL-01) , Mouse monoclonal to Serum Albumin, Isotype IgG1, Host Mouse 50 ug
AK8971 Human Serum Albumin- Low Folate and B12 Powder (Diagnostic Grade) Human Serum Albumin Inquire
AK8214 Human Serum Albumin 20 percent Solution (Diagnostic Grade) Human Serum Albumin Inquire
AK8228 Human Serum Albumin 25 percent Solution (Diagnostic Grade) Human Serum Albumin Inquire
AK8969 Human Serum Albumin 5 percent Solution (Diagnostic Grade) Human Serum Albumin Inquire
orb22396 Rabbit Serum Against Rat Albumin Polyclonal Precipitating polyclonal rabbit antiserum to rat serum albumin. As precipitating antiserum to identify or measure rat albumin by a variety of immunodiffusio 1 ml
orb21924 Goat Serum Against Cat Albumin Polyclonal Precipitating polyclonal goat antiserum to cat serum albumin. As precipitating antiserum to identify or measure cat albumin by a variety of immunodiffusion te 1 ml
orb22306 Rabbit Serum Against Dog Albumin Polyclonal Precipitating polyclonal rabbit antiserum to dog serum albumin. As precipitating antiserum to identify or measure dog albumin by a variety of immunodiffusio 1 ml
orb22183 Goat Serum Against Rat Albumin Polyclonal Precipitating polyclonal goat antiserum to rat serum albumin. As precipitating antiserum to identify or measure rat albumin by a variety of immunodiffusion te 1 ml
orb22191 Goat Serum Albumin Chromatographically purified goat albumin. Purified goat albumin may be used as a reference antigen, calibrator, coating protein and blocking agent in a variety of immunoassays incl 100 mg
ALBUMIN Liquid stable, BCG method for the determination of albumin in serum, plasma 1x150 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur