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

Apolipoprotein C-II (Apo-CII) (ApoC-II) (Apolipoprotein C2) [Cleaved into: Proapolipoprotein C-II (ProapoC-II)]

 APOC2_HUMAN             Reviewed;         101 AA.
P02655; C0JYY4; Q9BS39; Q9UDE3; Q9UNK3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
23-MAY-2018, entry version 201.
RecName: Full=Apolipoprotein C-II;
Short=Apo-CII;
Short=ApoC-II;
AltName: Full=Apolipoprotein C2;
Contains:
RecName: Full=Proapolipoprotein C-II;
Short=ProapoC-II;
Flags: Precursor;
Name=APOC2; Synonyms=APC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3030808; DOI=10.1016/0014-5793(87)81495-3;
Fojo S.S., Law S.W., Brewer H.B. Jr.;
"The human preproapolipoprotein C-II gene. Complete nucleic acid
sequence and genomic organization.";
FEBS Lett. 213:221-226(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6593704; DOI=10.1073/pnas.81.20.6354;
Fojo S.S., Law S.W., Brewer H.B. Jr.;
"Human apolipoprotein C-II: complete nucleic acid sequence of
preapolipoprotein C-II.";
Proc. Natl. Acad. Sci. U.S.A. 81:6354-6357(1984).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6328445; DOI=10.1093/nar/12.9.3917;
Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C.,
Baralle F.E.;
"Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA
abundance.";
Nucleic Acids Res. 12:3917-3932(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3558370;
Das H.K., Jackson C.L., Miller D.A., Leff T., Breslow J.L.;
"The human apolipoprotein C-II gene sequence contains a novel
chromosome 19-specific minisatellite in its third intron.";
J. Biol. Chem. 262:4787-4793(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=2415514;
Wei C.F., Tsao Y.K., Robberson D.L., Gotto A.M. Jr., Brown K.,
Chan L.;
"The structure of the human apolipoprotein C-II gene. Electron
microscopic analysis of RNA:DNA hybrids, complete nucleotide sequence,
and identification of 5' homologous sequences among apolipoprotein
genes.";
J. Biol. Chem. 260:15211-15221(1985).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H.,
Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[9]
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-101, AND TISSUE SPECIFICITY.
PubMed=6546757;
Myklebost O., Williamson B., Markham A.F., Myklebost S.R., Rogers J.,
Woods D.E., Humphries S.E.;
"The isolation and characterization of cDNA clones for human
apolipoprotein CII.";
J. Biol. Chem. 259:4401-4404(1984).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 11-101.
PubMed=3014272; DOI=10.1016/0076-6879(86)28106-9;
Jackson C.L., Bruns G.A.P., Breslow J.L.;
"Isolation of cDNA and genomic clones for apolipoprotein C-II.";
Methods Enzymol. 128:788-800(1986).
[13]
PROTEIN SEQUENCE OF 23-101.
PubMed=6706938;
Hospattankar A.V., Fairwell T., Ronan R., Brewer H.B. Jr.;
"Amino acid sequence of human plasma apolipoprotein C-II from normal
and hyperlipoproteinemic subjects.";
J. Biol. Chem. 259:318-322(1984).
[14]
PROTEIN SEQUENCE OF 23-101.
PubMed=194244; DOI=10.1073/pnas.74.5.1942;
Jackson R.L., Baker H.N., Gilliam E.B., Gotto A.M. Jr.;
"Primary structure of very low density apolipoprotein C-II of human
plasma.";
Proc. Natl. Acad. Sci. U.S.A. 74:1942-1945(1977).
[15]
PROTEIN SEQUENCE OF 29-35, PROTEOLYTIC PROCESSING, GLYCOSYLATION, AND
SUBCELLULAR LOCATION.
PubMed=3525527;
Fojo S.S., Taam L., Fairwell T., Ronan R., Bishop C., Meng M.S.,
Hoeg J.M., Sprecher D.L., Brewer H.B. Jr.;
"Human preproapolipoprotein C-II. Analysis of major plasma isoforms.";
J. Biol. Chem. 261:9591-9594(1986).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 77-101.
PubMed=11310852;
Chun E.M., Park Y.J., Kang H.S., Cho H.M., Jun D.Y., Kim Y.H.;
"Expression of the apolipoprotein C-II gene during myelomonocytic
differentiation of human leukemic cells.";
J. Leukoc. Biol. 69:645-650(2001).
[17]
REGION LIPOPROTEIN LIPASE COFACTOR AND REGION LIPID BINDING.
PubMed=6772077; DOI=10.1111/j.1749-6632.1980.tb21300.x;
Sparrow J.T., Gotto A.M. Jr.;
"Phospholipid binding studies with synthetic apolipoprotein
fragments.";
Ann. N. Y. Acad. Sci. 348:187-211(1980).
[18]
FUNCTION.
PubMed=2209608; DOI=10.1111/j.1432-1033.1990.tb19255.x;
Bengtsson-Olivecrona G., Sletten K.;
"Primary structure of the bovine analogues to human apolipoproteins
CII and CIII. Studies on isoforms and evidence for proteolytic
processing.";
Eur. J. Biochem. 192:515-521(1990).
[19]
REVIEW.
PubMed=22304839; DOI=10.1016/j.metabol.2011.12.002;
Kei A.A., Filippatos T.D., Tsimihodimos V., Elisaf M.S.;
"A review of the role of apolipoprotein C-II in lipoprotein metabolism
and cardiovascular disease.";
Metabolism 61:906-921(2012).
[20]
GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[21]
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).
[22]
STRUCTURE BY NMR OF 72-101, AND REGION LIPOPROTEIN LIPASE COFACTOR.
PubMed=1555583; DOI=10.1111/j.1432-1033.1992.tb16772.x;
Lycksell P.-O., Oehman A., Bengtsson-Olivecrona G., Johansson L.B.-A.,
Wijmenga S.S., Wernic D., Graeslund A.;
"Sequence specific 1H-NMR assignments and secondary structure of a
carboxy-terminal functional fragment of apolipoprotein CII.";
Eur. J. Biochem. 205:223-231(1992).
[23]
STRUCTURE BY NMR OF 72-101.
PubMed=8112221; DOI=10.1007/BF00213558;
Oehman A., Lycksell P.-O., Graeslund A.;
"A refined three-dimensional solution structure of a carboxy terminal
fragment of apolipoprotein CII.";
Eur. Biophys. J. 22:351-357(1993).
[24]
VARIANT AFRICA GLN-77.
PubMed=3944271; DOI=10.1172/JCI112342;
Menzel H.-J., Kane J.P., Malloy M.J., Havel R.J.;
"A variant primary structure of apolipoprotein C-II in individuals of
African descent.";
J. Clin. Invest. 77:595-601(1986).
[25]
VARIANT SAN FRANCISCO LYS-60.
PubMed=8490626; DOI=10.1093/hmg/2.1.69;
Pullinger C.R., Zysow B.R., Hennessy L.K., Frost P.H., Malloy M.J.,
Kanr J.P.;
"Molecular cloning and characteristics of a new apolipoprotein C-II
mutant identified in three unrelated individuals with
hypercholesterolemia and hypertriglyceridemia.";
Hum. Mol. Genet. 2:69-74(1993).
[26]
VARIANT THR-41.
PubMed=1782747;
Hegele R.A., Connelly P.W., Maguire G.F., Huff M.W., Leiter L.,
Wolfe B.M., Evans A.J., Little J.A.;
"An apolipoprotein CII mutation, CII Lys-19-->Thr identified in
patients with hyperlipidemia.";
Dis. Markers 9:73-80(1991).
[27]
VARIANT THR-41.
PubMed=7923858;
Zysow B.R., Pullinger C.R., Hennessy L.K., Farese R.V. Jr.,
Ghassemzadeh M., Kane J.P.;
"The apolipoprotein C-II variant apoC-II Lys-19-->Thr is not
associated with dyslipidemia in an affected kindred.";
Clin. Genet. 45:292-297(1994).
[28]
VARIANT HLPP1B WAKAYAMA ARG-48.
PubMed=8323539; DOI=10.1006/bbrc.1993.1749;
Inadera H., Hibino A., Kobayashi J., Kanzaki T., Shirai K., Yukawa S.,
Saito Y., Yoshida S.;
"A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein
CII gene in a patient with apolipoprotein CII deficiency (apo CII-
Wakayama).";
Biochem. Biophys. Res. Commun. 193:1174-1183(1993).
[29]
VARIANT GLN-77.
PubMed=10391210; DOI=10.1038/10297;
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
Cooper R., Lipshutz R., Chakravarti A.;
"Patterns of single-nucleotide polymorphisms in candidate genes for
blood-pressure homeostasis.";
Nat. Genet. 22:239-247(1999).
-!- FUNCTION: Component of chylomicrons, very low-density lipoproteins
(VLDL), low-density lipoproteins (LDL), and high-density
lipoproteins (HDL) in plasma. Plays an important role in
lipoprotein metabolism as an activator of lipoprotein lipase. Both
proapolipoprotein C-II and apolipoprotein C-II can activate
lipoprotein lipase. In normolipidemic individuals, it is mainly
distributed in the HDL, whereas in hypertriglyceridemic
individuals, predominantly found in the VLDL and LDL.
{ECO:0000269|PubMed:2209608, ECO:0000303|PubMed:22304839}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3525527}.
-!- TISSUE SPECIFICITY: Liver and intestine.
{ECO:0000269|PubMed:6546757}.
-!- PTM: Proapolipoprotein C-II is synthesized as a sialic acid
containing glycoprotein which is subsequently desialylated prior
to its proteolytic processing. {ECO:0000269|PubMed:3525527}.
-!- PTM: Proapolipoprotein C-II, the major form found in plasma
undergoes proteolytic cleavage of its N-terminal hexapeptide to
generate apolipoprotein C-II, which occurs as the minor form in
plasma. {ECO:0000269|PubMed:3525527}.
-!- DISEASE: Hyperlipoproteinemia 1B (HLPP1B) [MIM:207750]: Autosomal
recessive trait characterized by hypertriglyceridemia, xanthomas,
and increased risk of pancreatitis and early atherosclerosis.
{ECO:0000269|PubMed:8323539}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the apolipoprotein C2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X05151; CAA28798.1; -; Genomic_DNA.
EMBL; X00568; CAA25234.1; -; mRNA.
EMBL; J02698; AAA98743.1; -; Genomic_DNA.
EMBL; AY422955; AAQ91814.1; -; Genomic_DNA.
EMBL; BT006708; AAP35354.1; -; mRNA.
EMBL; FJ525875; ACN81313.1; -; Genomic_DNA.
EMBL; CH471126; EAW57311.1; -; Genomic_DNA.
EMBL; BC005348; AAH05348.3; -; mRNA.
EMBL; M29844; AAA51743.1; -; mRNA.
EMBL; M10612; AAB59380.1; -; Genomic_DNA.
EMBL; AF113884; AAD28193.1; -; mRNA.
CCDS; CCDS12650.1; -.
PIR; A24238; LPHUC2.
RefSeq; NP_000474.2; NM_000483.4.
UniGene; Hs.75615; -.
PDB; 1BY6; NMR; -; A=66-101.
PDB; 1I5J; NMR; -; A=23-101.
PDB; 1O8T; NMR; -; A=23-101.
PDB; 1SOH; NMR; -; A=23-101.
PDBsum; 1BY6; -.
PDBsum; 1I5J; -.
PDBsum; 1O8T; -.
PDBsum; 1SOH; -.
ProteinModelPortal; P02655; -.
SMR; P02655; -.
BioGrid; 106841; 4.
IntAct; P02655; 4.
STRING; 9606.ENSP00000466775; -.
iPTMnet; P02655; -.
PhosphoSitePlus; P02655; -.
BioMuta; APOC2; -.
DMDM; 114022; -.
DOSAC-COBS-2DPAGE; P02655; -.
SWISS-2DPAGE; P02655; -.
EPD; P02655; -.
MaxQB; P02655; -.
PaxDb; P02655; -.
PeptideAtlas; P02655; -.
PRIDE; P02655; -.
TopDownProteomics; P02655; -.
DNASU; 344; -.
Ensembl; ENST00000252490; ENSP00000252490; ENSG00000234906.
Ensembl; ENST00000590360; ENSP00000466775; ENSG00000234906.
GeneID; 344; -.
KEGG; hsa:344; -.
UCSC; uc060zuu.1; human.
CTD; 344; -.
DisGeNET; 344; -.
EuPathDB; HostDB:ENSG00000234906.8; -.
GeneCards; APOC2; -.
HGNC; HGNC:609; APOC2.
HPA; HPA055877; -.
MalaCards; APOC2; -.
MIM; 207750; phenotype.
MIM; 608083; gene.
neXtProt; NX_P02655; -.
OpenTargets; ENSG00000234906; -.
Orphanet; 309020; Familial apolipoprotein C-II deficiency.
PharmGKB; PA52; -.
eggNOG; ENOG410J3QQ; Eukaryota.
eggNOG; ENOG4111AXD; LUCA.
GeneTree; ENSGT00390000007913; -.
HOGENOM; HOG000034002; -.
HOVERGEN; HBG050548; -.
InParanoid; P02655; -.
KO; K22287; -.
OrthoDB; EOG091G17WL; -.
PhylomeDB; P02655; -.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-8964058; HDL remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; P02655; -.
EvolutionaryTrace; P02655; -.
GeneWiki; Apolipoprotein_C2; -.
GenomeRNAi; 344; -.
PMAP-CutDB; P02655; -.
PRO; PR:P02655; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000234906; -.
CleanEx; HS_APC2; -.
CleanEx; HS_APOC2; -.
ExpressionAtlas; P02655; baseline and differential.
Genevisible; P02655; HS.
GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0055102; F:lipase inhibitor activity; IDA:BHF-UCL.
GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:BHF-UCL.
GO; GO:0016004; F:phospholipase activator activity; IDA:BHF-UCL.
GO; GO:0043274; F:phospholipase binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IMP:BHF-UCL.
GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IC:BHF-UCL.
GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
GO; GO:0034382; P:chylomicron remnant clearance; IDA:BHF-UCL.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0034384; P:high-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; TAS:Reactome.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
GO; GO:0032375; P:negative regulation of cholesterol transport; IMP:BHF-UCL.
GO; GO:0045833; P:negative regulation of lipid metabolic process; IDA:BHF-UCL.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:BHF-UCL.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
GO; GO:0010518; P:positive regulation of phospholipase activity; IDA:BHF-UCL.
GO; GO:0060697; P:positive regulation of phospholipid catabolic process; IDA:BHF-UCL.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:BHF-UCL.
GO; GO:0010902; P:positive regulation of very-low-density lipoprotein particle remodeling; IC:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; TAS:BHF-UCL.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; TAS:BHF-UCL.
Gene3D; 1.10.1440.10; -; 1.
InterPro; IPR008019; Apo-CII.
InterPro; IPR023121; ApoC-II_dom_sf.
PANTHER; PTHR16566; PTHR16566; 1.
Pfam; PF05355; Apo-CII; 1.
1: Evidence at protein level;
3D-structure; Chylomicron; Complete proteome;
Direct protein sequencing; Disease mutation; Glycoprotein; HDL;
Hyperlipidemia; LDL; Lipid degradation; Lipid metabolism;
Lipid transport; Polymorphism; Reference proteome; Secreted;
Sialic acid; Signal; Transport; VLDL.
SIGNAL 1 22 {ECO:0000269|PubMed:194244,
ECO:0000269|PubMed:6706938}.
CHAIN 23 101 Proapolipoprotein C-II.
{ECO:0000269|PubMed:194244,
ECO:0000269|PubMed:6706938}.
/FTId=PRO_0000002024.
CHAIN 29 101 Apolipoprotein C-II.
{ECO:0000305|PubMed:3525527}.
/FTId=PRO_0000430839.
REGION 23 38 O-glycosylated at one site.
REGION 66 74 Lipid binding.
{ECO:0000269|PubMed:6772077}.
REGION 78 101 Lipoprotein lipase cofactor.
{ECO:0000269|PubMed:1555583,
ECO:0000269|PubMed:6772077}.
VARIANT 41 41 K -> T (in dbSNP:rs120074114).
{ECO:0000269|PubMed:1782747,
ECO:0000269|PubMed:7923858}.
/FTId=VAR_000639.
VARIANT 48 48 W -> R (in HLPP1B; variant Wakayama;
dbSNP:rs120074115).
{ECO:0000269|PubMed:8323539}.
/FTId=VAR_000640.
VARIANT 60 60 E -> K (in San Francisco; found in
hyperlipidemic patients; dbSNP:rs5122).
{ECO:0000269|PubMed:8490626}.
/FTId=VAR_000641.
VARIANT 77 77 K -> Q (in Africa; dbSNP:rs5126).
{ECO:0000269|PubMed:10391210,
ECO:0000269|PubMed:3944271}.
/FTId=VAR_000642.
CONFLICT 36 36 F -> L (in Ref. 7; AAP35354 and 8;
ACN81313). {ECO:0000305}.
STRAND 28 31 {ECO:0000244|PDB:1O8T}.
HELIX 37 57 {ECO:0000244|PDB:1I5J}.
TURN 58 61 {ECO:0000244|PDB:1I5J}.
STRAND 62 64 {ECO:0000244|PDB:1I5J}.
TURN 68 70 {ECO:0000244|PDB:1SOH}.
STRAND 71 74 {ECO:0000244|PDB:1I5J}.
TURN 75 77 {ECO:0000244|PDB:1BY6}.
TURN 79 81 {ECO:0000244|PDB:1BY6}.
STRAND 86 88 {ECO:0000244|PDB:1BY6}.
HELIX 92 94 {ECO:0000244|PDB:1BY6}.
HELIX 97 99 {ECO:0000244|PDB:1BY6}.
SEQUENCE 101 AA; 11284 MW; 51CB86FEDB174D84 CRC64;
MGTRLLPALF LVLLVLGFEV QGTQQPQQDE MPSPTFLTQV KESLSSYWES AKTAAQNLYE
KTYLPAVDEK LRDLYSKSTA AMSTYTGIFT DQVLSVLKGE E


Related products :

Catalog number Product name Quantity
E1890r ELISA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
E1890b ELISA kit APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
U0252m CLIA Apoc1,Apoc1b,Apo-CIB,ApoC-IB,Apolipoprotein C1,Apolipoprotein C-I,Mouse,Mus musculus 96T
E1890m ELISA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
E1890r ELISA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
U1890r CLIA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
U1890m CLIA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
E0252m ELISA kit Apoc1,Apoc1b,Apo-CIB,ApoC-IB,Apolipoprotein C1,Apolipoprotein C-I,Mouse,Mus musculus 96T
U1890b CLIA APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
E1890b ELISA APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
E1890m ELISA Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
U1890r CLIA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Rat,Rattus norvegicus 96T
U1890m CLIA kit Apoc3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Mouse,Mus musculus 96T
E0252m ELISA Apoc1,Apoc1b,Apo-CIB,ApoC-IB,Apolipoprotein C1,Apolipoprotein C-I,Mouse,Mus musculus 96T
U1890b CLIA kit APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Bos taurus,Bovine 96T
U1890p CLIA APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Pig,Sus scrofa 96T
U1996m CLIA kit Apoc2,Apo-CII,ApoC-II,Apolipoprotein C2,Apolipoprotein C-II,Mouse,Mus musculus 96T
U1996m CLIA Apoc2,Apo-CII,ApoC-II,Apolipoprotein C2,Apolipoprotein C-II,Mouse,Mus musculus 96T
E1890p ELISA kit APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Pig,Sus scrofa 96T
U1996b CLIA APOC2,Apo-CII,ApoC-II,Apolipoprotein C2,Apolipoprotein C-II,Bos taurus,Bovine 96T
E1996b ELISA kit APOC2,Apo-CII,ApoC-II,Apolipoprotein C2,Apolipoprotein C-II,Bos taurus,Bovine 96T
U1996b CLIA kit APOC2,Apo-CII,ApoC-II,Apolipoprotein C2,Apolipoprotein C-II,Bos taurus,Bovine 96T
E1996b ELISA APOC2,Apo-CII,ApoC-II,Apolipoprotein C2,Apolipoprotein C-II,Bos taurus,Bovine 96T
U1890p CLIA kit APOC3,Apo-CIII,ApoC-III,Apolipoprotein C3,Apolipoprotein C-III,Pig,Sus scrofa 96T
E1996m ELISA kit Apoc2,Apo-CII,ApoC-II,Apolipoprotein C2,Apolipoprotein C-II,Mouse,Mus musculus 96T


 

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