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Serotransferrin (Transferrin) (Beta-1 metal-binding globulin) (Siderophilin)

 TRFE_MOUSE              Reviewed;         697 AA.
Q921I1; O35421; Q3UBW7; Q58E69; Q61803; Q62357; Q62358; Q62359;
Q63915; Q64515; Q8VII5; Q922C0;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-DEC-2018, entry version 166.
RecName: Full=Serotransferrin;
Short=Transferrin;
AltName: Full=Beta-1 metal-binding globulin;
AltName: Full=Siderophilin;
Flags: Precursor;
Name=Tf; Synonyms=Trf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
Lai D.-Z.;
"Construction of a robust CHO cell-line for biopharmaceutical
production.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Liver, and Mammary gland;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
STRAIN=BALB/cJ;
PubMed=9621303;
DOI=10.1002/(SICI)1098-2795(199807)50:3<273::AID-MRD3>3.0.CO;2-G;
Chaudhary J., Skinner M.K.;
"Comparative sequence analysis of the mouse and human transferrin
promoters: hormonal regulation of the transferrin promoter in Sertoli
cells.";
Mol. Reprod. Dev. 50:273-283(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 66-131; 277-337; 462-496 AND 526-575.
PubMed=3693348;
Chen L.-H., Bissell M.J.;
"Transferrin mRNA level in the mouse mammary gland is regulated by
pregnancy and extracellular matrix.";
J. Biol. Chem. 262:17247-17250(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 268-307.
TISSUE=Placenta;
PubMed=8248032; DOI=10.1016/S0143-4004(05)80458-8;
Kasik J.W., Rice E.J.;
"Transferrin gene expression in maternal liver, fetal liver and
placenta during pregnancy in the mouse.";
Placenta 14:365-371(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 282-412.
PubMed=3611056;
Pentecost B.T., Teng C.T.;
"Lactotransferrin is the major estrogen inducible protein of mouse
uterine secretions.";
J. Biol. Chem. 262:10134-10139(1987).
[8]
PROTEIN SEQUENCE OF 332-343 AND 659-667, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[9]
TISSUE SPECIFICITY.
PubMed=2601714; DOI=10.1128/MCB.9.11.5154;
Idzerda R.L., Behringer R.R., Theisen M., Huggenvik J.I.,
McKnight G.S., Brinster R.L.;
"Expression from the transferrin gene promoter in transgenic mice.";
Mol. Cell. Biol. 9:5154-5162(1989).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-513.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Transferrins are iron binding transport proteins which
can bind two Fe(3+) ions in association with the binding of an
anion, usually bicarbonate. It is responsible for the transport of
iron from sites of absorption and heme degradation to those of
storage and utilization. Serum transferrin may also have a further
role in stimulating cell proliferation.
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
{ECO:0000269|PubMed:2601714}.
-!- SIMILARITY: Belongs to the transferrin family.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
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EMBL; AF440692; AAL34533.1; -; mRNA.
EMBL; AK085754; BAC39532.1; -; mRNA.
EMBL; AK142599; BAE25124.1; -; mRNA.
EMBL; AK146549; BAE27253.1; -; mRNA.
EMBL; AK149559; BAE28960.1; -; mRNA.
EMBL; AK149595; BAE28981.1; -; mRNA.
EMBL; AK150782; BAE29847.1; -; mRNA.
EMBL; AK168419; BAE40332.1; -; mRNA.
EMBL; AK168938; BAE40747.1; -; mRNA.
EMBL; BC008559; AAH08559.1; -; mRNA.
EMBL; BC012313; AAH12313.1; -; mRNA.
EMBL; BC022986; AAH22986.1; -; mRNA.
EMBL; BC092046; AAH92046.1; -; mRNA.
EMBL; AF027336; AAB84034.1; -; Genomic_DNA.
EMBL; M23013; AAA40488.1; -; mRNA.
EMBL; M23014; AAA40489.1; -; mRNA.
EMBL; M23015; AAA40490.1; -; mRNA.
EMBL; M23016; AAA40491.1; -; mRNA.
EMBL; S67217; AAB28966.2; -; mRNA.
EMBL; J03299; AAA39438.1; -; mRNA.
CCDS; CCDS23451.1; -.
PIR; A28446; A28446.
RefSeq; NP_598738.1; NM_133977.2.
UniGene; Mm.37214; -.
ProteinModelPortal; Q921I1; -.
SMR; Q921I1; -.
BioGrid; 204313; 1.
IntAct; Q921I1; 8.
MINT; Q921I1; -.
STRING; 10090.ENSMUSP00000035158; -.
MEROPS; S60.972; -.
CarbonylDB; Q921I1; -.
GlyConnect; 556; -.
iPTMnet; Q921I1; -.
PhosphoSitePlus; Q921I1; -.
SwissPalm; Q921I1; -.
REPRODUCTION-2DPAGE; IPI00139788; -.
REPRODUCTION-2DPAGE; Q921I1; -.
MaxQB; Q921I1; -.
PaxDb; Q921I1; -.
PeptideAtlas; Q921I1; -.
PRIDE; Q921I1; -.
Ensembl; ENSMUST00000035158; ENSMUSP00000035158; ENSMUSG00000032554.
Ensembl; ENSMUST00000112645; ENSMUSP00000108264; ENSMUSG00000032554.
GeneID; 22041; -.
KEGG; mmu:22041; -.
UCSC; uc009rgj.1; mouse.
CTD; 22041; -.
MGI; MGI:98821; Trf.
eggNOG; ENOG410IEAI; Eukaryota.
eggNOG; ENOG410XQ36; LUCA.
GeneTree; ENSGT00940000154388; -.
HOVERGEN; HBG000055; -.
InParanoid; Q921I1; -.
KO; K14736; -.
OMA; CTVSSHE; -.
OrthoDB; EOG091G0242; -.
PhylomeDB; Q921I1; -.
TreeFam; TF324013; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
Reactome; R-MMU-917937; Iron uptake and transport.
Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
ChiTaRS; Trf; mouse.
PRO; PR:Q921I1; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032554; Expressed in 44 organ(s), highest expression level in liver.
CleanEx; MM_TRF; -.
ExpressionAtlas; Q921I1; baseline and differential.
Genevisible; Q921I1; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0045178; C:basal part of cell; ISO:MGI.
GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
GO; GO:0005604; C:basement membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0051286; C:cell tip; ISO:MGI.
GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0097433; C:dense body; ISO:MGI.
GO; GO:0005769; C:early endosome; IDA:MGI.
GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; ISO:MGI.
GO; GO:1990712; C:HFE-transferrin receptor complex; ISO:MGI.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0055037; C:recycling endosome; IDA:MGI.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0030120; C:vesicle coat; ISO:MGI.
GO; GO:0008199; F:ferric iron binding; ISO:MGI.
GO; GO:0015091; F:ferric iron transmembrane transporter activity; IEA:InterPro.
GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
GO; GO:0034986; F:iron chaperone activity; ISO:MGI.
GO; GO:1990459; F:transferrin receptor binding; ISO:MGI.
GO; GO:0007015; P:actin filament organization; IDA:DFLAT.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:DFLAT.
GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
GO; GO:0071281; P:cellular response to iron ion; ISO:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:DFLAT.
GO; GO:0015682; P:ferric iron transport; ISO:MGI.
GO; GO:0006826; P:iron ion transport; IMP:MGI.
GO; GO:0030316; P:osteoclast differentiation; IDA:DFLAT.
GO; GO:0045780; P:positive regulation of bone resorption; IDA:DFLAT.
GO; GO:2000147; P:positive regulation of cell motility; IDA:DFLAT.
GO; GO:0031643; P:positive regulation of myelination; ISO:MGI.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; ISO:MGI.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:DFLAT.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:DFLAT.
GO; GO:1900390; P:regulation of iron ion import; ISO:MGI.
GO; GO:0009617; P:response to bacterium; IEP:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
InterPro; IPR030685; Serotransferrin_mammal.
InterPro; IPR016357; Transferrin.
InterPro; IPR001156; Transferrin-like_dom.
InterPro; IPR018195; Transferrin_Fe_BS.
Pfam; PF00405; Transferrin; 2.
PIRSF; PIRSF500682; Serotransferrin; 1.
PIRSF; PIRSF002549; Transferrin; 1.
PRINTS; PR00422; TRANSFERRIN.
SMART; SM00094; TR_FER; 2.
PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Ion transport; Iron; Iron transport; Metal-binding;
Methylation; Phosphoprotein; Reference proteome; Repeat; Secreted;
Signal; Transport.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 697 Serotransferrin.
/FTId=PRO_0000035716.
DOMAIN 25 347 Transferrin-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
DOMAIN 360 682 Transferrin-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 82 82 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 114 114 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 207 207 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 268 268 Iron 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 410 410 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 448 448 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 537 537 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
METAL 605 605 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 139 139 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 143 143 Carbonate 1. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 145 145 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 146 146 Carbonate 1; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 474 474 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 478 478 Carbonate 2. {ECO:0000255|PROSITE-
ProRule:PRU00741}.
BINDING 480 480 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
BINDING 481 481 Carbonate 2; via amide nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00741}.
MOD_RES 42 42 Dimethylated arginine.
{ECO:0000250|UniProtKB:P12346}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:P02787}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
DISULFID 28 67 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 38 58 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 137 213 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 156 350 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 177 193 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 180 196 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 190 198 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 246 260 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 363 395 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 373 386 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 420 692 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 435 655 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 472 543 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 496 683 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 506 520 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 517 526 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 583 597 {ECO:0000255|PROSITE-ProRule:PRU00741}.
DISULFID 633 638 {ECO:0000255|PROSITE-ProRule:PRU00741}.
CONFLICT 3 4 LT -> FA (in Ref. 1; AAL34533).
{ECO:0000305}.
CONFLICT 69 69 K -> R (in Ref. 5; AAA40488).
{ECO:0000305}.
CONFLICT 71 74 ISAS -> HASG (in Ref. 3; AAH08559).
{ECO:0000305}.
CONFLICT 72 72 S -> A (in Ref. 5; AAA40488).
{ECO:0000305}.
CONFLICT 85 85 W -> L (in Ref. 5; AAA40488).
{ECO:0000305}.
CONFLICT 104 104 Y -> C (in Ref. 5; AAA40488).
{ECO:0000305}.
CONFLICT 113 113 Y -> S (in Ref. 5; AAA40488).
{ECO:0000305}.
CONFLICT 123 124 GT -> ER (in Ref. 5; AAA40488).
{ECO:0000305}.
CONFLICT 135 135 K -> E (in Ref. 2; BAE29847).
{ECO:0000305}.
CONFLICT 283 283 W -> L (in Ref. 6; AAB28966).
{ECO:0000305}.
CONFLICT 307 307 P -> L (in Ref. 6; AAB28966).
{ECO:0000305}.
CONFLICT 350 351 CP -> SA (in Ref. 7; AAA39438).
{ECO:0000305}.
CONFLICT 487 487 G -> C (in Ref. 5; AAA40490).
{ECO:0000305}.
CONFLICT 527 527 A -> D (in Ref. 5; AAA40491).
{ECO:0000305}.
CONFLICT 529 529 N -> S (in Ref. 2; BAE29847).
{ECO:0000305}.
CONFLICT 575 575 K -> N (in Ref. 5; AAA40491).
{ECO:0000305}.
CONFLICT 697 697 H -> S (in Ref. 1; AAL34533).
{ECO:0000305}.
SEQUENCE 697 AA; 76724 MW; 0996A0C3B64CB1B9 CRC64;
MRLTVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP PDGPRLACVK
KTSYPDCIKA ISASEADAMT LDGGWVYDAG LTPNNLKPVA AEFYGSVEHP QTYYYAVAVV
KKGTDFQLNQ LEGKKSCHTG LGRSAGWVIP IGLLFCKLSE PRSPLEKAVS SFFSGSCVPC
ADPVAFPKLC QLCPGCGCSS TQPFFGYVGA FKCLKDGGGD VAFVKHTTIF EVLPEKADRD
QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARKNNGKED LIWEILKVAQ EHFGKGKSKD
FQLFSSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHNYVT AIRNQQEGVC PEGSIDNSPV
KWCALSHLER TKCDEWSIIS EGKIECESAE TTEDCIEKIV NGEADAMTLD GGHAYIAGQC
GLVPVMAEYY ESSNCAIPSQ QGIFPKGYYA VAVVKASDTS ITWNNLKGKK SCHTGVDRTA
GWNIPMGMLY NRINHCKFDE FFSQGCAPGY EKNSTLCDLC IGPLKCAPNN KEEYNGYTGA
FRCLVEKGDV AFVKHQTVLD NTEGKNPAEW AKNLKQEDFE LLCPDGTRKP VKDFASCHLA
QAPNHVVVSR KEKAARVKAV LTSQETLFGG SDCTGNFCLF KSTTKDLLFR DDTKCFVKLP
EGTTPEKYLG AEYMQSVGNM RKCSTSRLLE ACTFHKH


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E2036m ELISA Beta-1 metal-binding globulin,Mouse,Mus musculus,Serotransferrin,Siderophilin,Tf,Transferrin,Trf 96T
E2036b ELISA Beta-1 metal-binding globulin,Bos taurus,Bovine,Serotransferrin,Siderophilin,TF,Transferrin 96T
E2036Rb ELISA kit Beta-1 metal-binding globulin,Oryctolagus cuniculus,Rabbit,Serotransferrin,Siderophilin,TF,Transferrin 96T
E2036Rb ELISA Beta-1 metal-binding globulin,Oryctolagus cuniculus,Rabbit,Serotransferrin,Siderophilin,TF,Transferrin 96T
U2036Rb CLIA kit Beta-1 metal-binding globulin,Oryctolagus cuniculus,Rabbit,Serotransferrin,Siderophilin,TF,Transferrin 96T
U2036Rb CLIA Beta-1 metal-binding globulin,Oryctolagus cuniculus,Rabbit,Serotransferrin,Siderophilin,TF,Transferrin 96T
U2036h CLIA kit Beta-1 metal-binding globulin,Homo sapiens,Human,PRO1400,Serotransferrin,Siderophilin,TF,Transferrin 96T
U2036h CLIA Beta-1 metal-binding globulin,Homo sapiens,Human,PRO1400,Serotransferrin,Siderophilin,TF,Transferrin 96T
E2036h ELISA Beta-1 metal-binding globulin,Homo sapiens,Human,PRO1400,Serotransferrin,Siderophilin,TF,Transferrin 96T
E2036h ELISA kit Beta-1 metal-binding globulin,Homo sapiens,Human,PRO1400,Serotransferrin,Siderophilin,TF,Transferrin 96T
E2036r ELISA Beta-1 metal-binding globulin,Liver regeneration-related protein LRRG03,Rat,Rattus norvegicus,Serotransferrin,Siderophilin,Tf,Transferrin 96T
E2036r ELISA kit Beta-1 metal-binding globulin,Liver regeneration-related protein LRRG03,Rat,Rattus norvegicus,Serotransferrin,Siderophilin,Tf,Transferrin 96T
U2036r CLIA kit Beta-1 metal-binding globulin,Liver regeneration-related protein LRRG03,Rat,Rattus norvegicus,Serotransferrin,Siderophilin,Tf,Transferrin 96T
U2036r CLIA Beta-1 metal-binding globulin,Liver regeneration-related protein LRRG03,Rat,Rattus norvegicus,Serotransferrin,Siderophilin,Tf,Transferrin 96T


 

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