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Collagen alpha-1(I) chain (Alpha-1 type I collagen)

 CO1A1_MOUSE             Reviewed;        1453 AA.
P11087; Q53WT0; Q60635; Q61367; Q61427; Q63919; Q6PCL3; Q810J9;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 4.
07-JUN-2017, entry version 177.
RecName: Full=Collagen alpha-1(I) chain;
AltName: Full=Alpha-1 type I collagen;
Flags: Precursor;
Name=Col1a1; Synonyms=Cola1;
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] (ISOFORM 1).
STRAIN=FVB/N;
PubMed=8535610; DOI=10.1016/S0945-053X(05)80009-5;
Li S.W., Khillan J., Prockop D.J.;
"The complete cDNA coding sequence for the mouse pro alpha 1(I) chain
of type I procollagen.";
Matrix Biol. 14:593-595(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=FVB/N; TISSUE=Colon;
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 1-25.
PubMed=6324198; DOI=10.1073/pnas.81.5.1504;
Harbers K., Kuehn M., Delius H., Jaenisch R.;
"Insertion of retrovirus into the first intron of alpha1(I) collagen
gene leads to embryonic lethal mutation in mice.";
Proc. Natl. Acad. Sci. U.S.A. 81:1504-1508(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 AND 1030-1453.
PubMed=8268229; DOI=10.1016/0167-4781(93)90016-7;
Fenton S.P., Lamande S.R., Hannagan M., Stacey A., Jaenisch R.,
Bateman J.F.;
"Genomic sequence of mouse COL1A1 encoding the collagen propeptides.";
Biochim. Biophys. Acta 1216:469-474(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-942.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=8065328; DOI=10.1128/MCB.14.9.5950;
Rhodes K., Rippe R.A., Umezawa A., Nehls M., Brenner D.A., Breindl M.;
"DNA methylation represses the murine alpha 1(I) collagen promoter by
an indirect mechanism.";
Mol. Cell. Biol. 14:5950-5960(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 518-1128 (ISOFORM 1).
PubMed=3841523; DOI=10.1016/0378-1119(85)90329-4;
French B.T., Lee W.-H., Maul G.G.;
"Nucleotide sequence of a cDNA clone for mouse pro alpha 1(I) collagen
protein.";
Gene 39:311-312(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 735-1130.
PubMed=6298597; DOI=10.1128/MCB.2.11.1362;
Monson J.M., Friedman J., McCarthy B.J.;
"DNA sequence analysis of a mouse pro alpha 1 (I) procollagen gene:
evidence for a mouse B1 element within the gene.";
Mol. Cell. Biol. 2:1362-1371(1982).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 735-878 AND 1005-1058.
PubMed=6219867; DOI=10.1089/dna.1.1981.1.59;
Monson J.M., McCarthy B.J.;
"Identification of a Balb/c mouse pro alpha 1(I) procollagen gene:
evidence for insertions or deletions in gene coding sequences.";
DNA 1:59-69(1981).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1442-1453.
PubMed=3340560; DOI=10.1093/nar/16.2.773;
Mooslehner K., Harbers K.;
"Two mRNAs of mouse pro alpha 1(I) collagen gene differ in the size of
the 3'-untranslated region.";
Nucleic Acids Res. 16:773-773(1988).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1442-1453.
PubMed=2054384;
Metsaeranta M., Toman D., de Crombrugghe B., Vuorio E.;
"Specific hybridization probes for mouse type I, II, III and IX
collagen mRNAs.";
Biochim. Biophys. Acta 1089:241-243(1991).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1354.
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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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: Type I collagen is a member of group I collagen
(fibrillar forming collagen).
-!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
Interacts with MRC2. Interacts with TRAM2. Interacts with MFAP4 in
a Ca (2+)-dependent manner. {ECO:0000250|UniProtKB:P02452,
ECO:0000250|UniProtKB:P02453, ECO:0000250|UniProtKB:P02454}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11087-1; Sequence=Displayed;
Name=2;
IsoId=P11087-2; Sequence=VSP_016548;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and
bones. In bones the fibrils are mineralized with calcium
hydroxyapatite.
-!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
have crucial roles in tissue growth and repair by controlling both
the intracellular assembly of procollagen molecules and the
extracellular assembly of collagen fibrils. It binds a calcium ion
which is essential for its function (By similarity).
{ECO:0000250}.
-!- PTM: Proline residues at the third position of the tripeptide
repeating unit (G-X-P) are hydroxylated in some or all of the
chains. Proline residues at the second position of the tripeptide
repeating unit (G-P-X) are hydroxylated in some of the chains.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- SEQUENCE CAUTION:
Sequence=CAA38657.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; U08020; AAA88912.1; -; mRNA.
EMBL; AL662790; CAI25880.1; -; Genomic_DNA.
EMBL; AL606480; CAI25880.1; JOINED; Genomic_DNA.
EMBL; AL606480; CAI23970.1; -; Genomic_DNA.
EMBL; AL662790; CAI23970.1; JOINED; Genomic_DNA.
EMBL; BC050014; AAH50014.1; -; mRNA.
EMBL; BC059281; AAH59281.1; -; mRNA.
EMBL; K01688; AAA37330.1; -; Genomic_DNA.
EMBL; S67530; AAB29424.1; -; Genomic_DNA.
EMBL; S67482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X54876; CAA38657.1; ALT_SEQ; Genomic_DNA.
EMBL; M14423; AAA37333.1; -; mRNA.
EMBL; M17491; AAA37334.1; -; Genomic_DNA.
EMBL; K03036; AAA37332.1; -; Genomic_DNA.
EMBL; K03029; AAA37332.1; JOINED; Genomic_DNA.
EMBL; K03030; AAA37332.1; JOINED; Genomic_DNA.
EMBL; K03031; AAA37332.1; JOINED; Genomic_DNA.
EMBL; K03032; AAA37332.1; JOINED; Genomic_DNA.
EMBL; K03033; AAA37332.1; JOINED; Genomic_DNA.
EMBL; K03034; AAA37332.1; JOINED; Genomic_DNA.
EMBL; K03035; AAA37332.1; JOINED; Genomic_DNA.
EMBL; X06753; CAA29927.1; -; Genomic_DNA.
EMBL; X15896; CAA33904.1; -; Genomic_DNA.
EMBL; X57981; CAA41046.1; -; Genomic_DNA.
CCDS; CCDS25265.1; -. [P11087-1]
PIR; I49558; I49558.
PIR; S57243; S21626.
RefSeq; NP_031768.2; NM_007742.4. [P11087-1]
UniGene; Mm.277735; -.
UniGene; Mm.458212; -.
ProteinModelPortal; P11087; -.
SMR; P11087; -.
BioGrid; 198831; 9.
IntAct; P11087; 2.
MINT; MINT-4091294; -.
STRING; 10090.ENSMUSP00000001547; -.
iPTMnet; P11087; -.
PhosphoSitePlus; P11087; -.
MaxQB; P11087; -.
PaxDb; P11087; -.
PeptideAtlas; P11087; -.
PRIDE; P11087; -.
Ensembl; ENSMUST00000001547; ENSMUSP00000001547; ENSMUSG00000001506. [P11087-1]
GeneID; 12842; -.
KEGG; mmu:12842; -.
UCSC; uc007kzn.1; mouse. [P11087-1]
CTD; 1277; -.
MGI; MGI:88467; Col1a1.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00840000129673; -.
HOVERGEN; HBG004933; -.
InParanoid; P11087; -.
KO; K06236; -.
OMA; FQFEYGS; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P11087; -.
TreeFam; TF344135; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1442490; Collagen degradation.
Reactome; R-MMU-1474244; Extracellular matrix organization.
Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-216083; Integrin cell surface interactions.
Reactome; R-MMU-2214320; Anchoring fibril formation.
Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-MMU-3000178; ECM proteoglycans.
Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
Reactome; R-MMU-76009; Platelet Aggregation (Plug Formation).
Reactome; R-MMU-8874081; MET activates PTK2 signaling.
Reactome; R-MMU-8948216; Collagen chain trimerization.
ChiTaRS; Col1a1; mouse.
PMAP-CutDB; P11087; -.
PRO; PR:P11087; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000001506; -.
CleanEx; MM_COL1A1; -.
Genevisible; P11087; MM.
GO; GO:0005581; C:collagen trimer; IDA:MGI.
GO; GO:0005584; C:collagen type I trimer; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0005201; F:extracellular matrix structural constituent; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0060346; P:bone trabecula formation; IGI:MGI.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
GO; GO:1902618; P:cellular response to fluoride; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0071306; P:cellular response to vitamin E; IEA:Ensembl.
GO; GO:0032964; P:collagen biosynthetic process; ISO:MGI.
GO; GO:0030199; P:collagen fibril organization; ISO:MGI.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; ISO:MGI.
GO; GO:0048706; P:embryonic skeletal system development; ISO:MGI.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:0060325; P:face morphogenesis; IGI:MGI.
GO; GO:0001957; P:intramembranous ossification; IGI:MGI.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IDA:MGI.
GO; GO:0001649; P:osteoblast differentiation; IEP:BHF-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0070208; P:protein heterotrimerization; IDA:MGI.
GO; GO:0034504; P:protein localization to nucleus; ISO:MGI.
GO; GO:0015031; P:protein transport; IMP:MGI.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
GO; GO:0001501; P:skeletal system development; IMP:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IGI:MGI.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0043589; P:skin morphogenesis; ISO:MGI.
GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
GO; GO:0034505; P:tooth mineralization; ISO:MGI.
GO; GO:0007601; P:visual perception; ISO:MGI.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR001007; VWF_dom.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 9.
Pfam; PF00093; VWC; 1.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00214; VWC; 1.
PROSITE; PS51461; NC1_FIB; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Collagen; Complete proteome;
Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
Metal-binding; Phosphoprotein; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 22
PROPEP 23 151 N-terminal propeptide.
/FTId=PRO_0000005722.
CHAIN 152 1207 Collagen alpha-1(I) chain.
/FTId=PRO_0000005723.
PROPEP 1208 1453 C-terminal propeptide.
/FTId=PRO_0000005724.
DOMAIN 29 87 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 1218 1453 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 152 167 Nonhelical region (N-terminal).
REGION 168 1181 Triple-helical region.
REGION 1182 1207 Nonhelical region (C-terminal).
MOTIF 734 736 Cell attachment site. {ECO:0000255}.
MOTIF 1082 1084 Cell attachment site. {ECO:0000255}.
METAL 1266 1266 Calcium. {ECO:0000250}.
METAL 1268 1268 Calcium. {ECO:0000250}.
METAL 1269 1269 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1271 1271 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1274 1274 Calcium. {ECO:0000250}.
MOD_RES 152 152 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P02453}.
MOD_RES 160 160 Allysine. {ECO:0000250|UniProtKB:P02452}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 254 254 5-hydroxylysine; alternate.
{ECO:0000250}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 776 776 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 1153 1153 3-hydroxyproline. {ECO:0000250}.
MOD_RES 1197 1197 Allysine. {ECO:0000250|UniProtKB:P02452}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 254 254 O-linked (Gal...) hydroxylysine;
alternate. {ECO:0000250}.
CARBOHYD 1354 1354 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
DISULFID 1248 1280 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1254 1254 Interchain (with C-1271).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1271 1271 Interchain (with C-1254).
{ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1288 1451 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1359 1404 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VAR_SEQ 803 1030 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016548.
CONFLICT 81 81 E -> G (in Ref. 1; AAA88912).
{ECO:0000305}.
CONFLICT 106 106 D -> G (in Ref. 1; AAA88912).
{ECO:0000305}.
CONFLICT 136 136 P -> H (in Ref. 3; AAH59281).
{ECO:0000305}.
CONFLICT 1202 1202 G -> D (in Ref. 1; AAA88912).
{ECO:0000305}.
CONFLICT 1219 1219 E -> A (in Ref. 1; AAA88912).
{ECO:0000305}.
CONFLICT 1222 1222 T -> A (in Ref. 1; AAA88912).
{ECO:0000305}.
CONFLICT 1335 1335 A -> T (in Ref. 1; AAA88912).
{ECO:0000305}.
CONFLICT 1399 1400 TL -> RV (in Ref. 1; AAA88912).
{ECO:0000305}.
CONFLICT 1450 1450 A -> V (in Ref. 10; CAA29927/CAA33904).
{ECO:0000305}.
SEQUENCE 1453 AA; 138032 MW; 0B7F06BBB9A1D5EA CRC64;
MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPEVCL ICICHNGTAV
CDDVQCNEEL DCPNPQRREG ECCAFCPEEY VSPNSEDVGV EGPKGDPGPQ GPRGPVGPPG
RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG
PPGAPGPQGF QGPPGEPGEP GGSGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG
ARGLPGTAGL PGMKGHRGFS GLDGAKGDAG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
RPGPPGTAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAVGA KGEAGPQGAR GSEGPQGVRG
EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ GPSGPPGPKG
NSGEPGAPGN KGDTGAKGEP GATGVQGPPG PAGEEGKRGA RGEPGPSGLP GPPGERGGPG
SRGFPGADGV AGPKGPSGER GAPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG
KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGLP GPPGAVGPAG
KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ GVPGDLGAPG
PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD TGAPGAPGSQ GAPGLQGMPG
ERGAAGLPGP KGDRGDAGPK GADGSPGKDG ARGLTGPIGP PGPAGAPGDK GEAGPSGPPG
PTGARGAPGD RGEAGPPGPA GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG
PIGNVGAPGP KGPRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG
ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV GLPGQRGERG
FPGLPGPSGE PGKQGPSGSS GERGPPGPMG PPGLAGPPGE SGREGSPGAE GSPGRDGAPG
AKGDRGETGP AGPPGAPGAP GAPGPVGPAG KNGDRGETGP AGPAGPIGPA GARGPAGPQG
PRGDKGETGE QGDRGIKGHR GFSGLQGPPG SPGSPGEQGP SGASGPAGPR GPPGSAGSPG
KDGLNGLPGP IGPPGPRGRT GDSGPAGPPG PPGPPGPPGP PSGGYDFSFL PQPPQEKSQD
GGRYYRADDA NVVRDRDLEV DTTLKSLSQQ IENIRSPEGS RKNPARTCRD LKMCHSDWKS
GEYWIDPNQG CNLDAIKVYC NMETGQTCVF PTQPSVPQKN WYISPNPKEK KHVWFGESMT
DGFPFEYGSE GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKALLLQ
GSNEIELRGE GNSRFTYSTL VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD
QEFGLDIGPA CFV


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E0571Rb ELISA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T
U0572h CLIA Alpha-1 type II collagen,COL2A1,Collagen alpha-1(II) chain,Homo sapiens,Human 96T
E0571Rb ELISA kit Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T
E0572h ELISA kit Alpha-1 type II collagen,COL2A1,Collagen alpha-1(II) chain,Homo sapiens,Human 96T
U0571Rb CLIA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Oryctolagus cuniculus,Rabbit 96T
E0571h ELISA kit Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
U0571m CLIA Alpha-1 type I collagen,Col1a1,Cola1,Collagen alpha-1(I) chain,Mouse,Mus musculus 96T
E0572h ELISA Alpha-1 type II collagen,COL2A1,Collagen alpha-1(II) chain,Homo sapiens,Human 96T
U0571h CLIA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
EIAAB08376 Alpha-2 type I collagen,COL1A2,Collagen alpha-2(I) chain,Oryctolagus cuniculus,Rabbit
AM10160PU-N Collagen type V (collagen v alpha-1 chain) (alpha-1) Mouse IgG1 antibody Ab Purified 0.1 mg
EIAAB08377 Alpha-2 type I collagen,Col1a2,Cola2,Collagen alpha-2(I) chain,Mouse,Mus musculus
'AM10160PU-N Collagen type V (collagen v alpha-1 chain) (alpha-1) IgG1 antibody Ab host: Mouse 0.1 mg
E0571r ELISA Alpha-1 type I collagen,Col1a1,Collagen alpha-1(I) chain,Rat,Rattus norvegicus 96T
U0572r CLIA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Rat,Rattus norvegicus 96T
E0572r ELISA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Rat,Rattus norvegicus 96T
E0572m ELISA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Mouse,Mus musculus 96T
E0572b ELISA Alpha-1 type II collagen,Bos taurus,Bovine,COL2A1,Collagen alpha-1(II) chain 96T
U0572b CLIA Alpha-1 type II collagen,Bos taurus,Bovine,COL2A1,Collagen alpha-1(II) chain 96T
EIAAB08374 Alpha-2 type I collagen,COL1A2,Collagen alpha-2(I) chain,Homo sapiens,Human
E0571r ELISA kit Alpha-1 type I collagen,Col1a1,Collagen alpha-1(I) chain,Rat,Rattus norvegicus 96T
E0571b ELISA Alpha-1 type I collagen,Bos taurus,Bovine,COL1A1,Collagen alpha-1(I) chain 96T


 

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