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

 CO1A1_RAT               Reviewed;        1453 AA.
P02454; A3KNA1; P02455; Q63079;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 5.
07-JUN-2017, entry version 156.
RecName: Full=Collagen alpha-1(I) chain;
AltName: Full=Alpha-1 type I collagen;
Flags: Precursor;
Name=Col1a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Bone, and Tooth;
PubMed=10065941; DOI=10.1177/00220345990780010101;
Brandsten C., Lundmark C., Christersson C., Hammarstroem L., Wurtz T.;
"Expression of collagen alpha1(I) mRNA variants during tooth and bone
formation in the rat.";
J. Dent. Res. 78:11-19(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Brown Norway; TISSUE=Lung;
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]
PROTEIN SEQUENCE OF 152-170, ALLYSINE AT LYS-160, AND PYROGLUTAMATE
FORMATION AT GLN-152.
PubMed=5777344; DOI=10.1021/bi00829a010;
Bornstein P.;
"Comparative sequence studies of rat skin and tendon collagen. II. The
absence of a short sequence at the amino terminus of the skin alpha-1
chain.";
Biochemistry 8:63-71(1969).
[5]
PROTEIN SEQUENCE OF 156-170.
PubMed=5337886; DOI=10.1021/bi00855a019;
Kang A.H., Bornstein P., Piez K.A.;
"The amino acid sequence of peptides from the cross-linking region of
rat skin collagen.";
Biochemistry 6:788-795(1967).
[6]
PROTEIN SEQUENCE OF 171-206.
PubMed=4290711;
Bornstein P.;
"The incomplete hydroxylation of individual prolyl residues in
collagen.";
J. Biol. Chem. 242:2572-2574(1967).
[7]
PROTEIN SEQUENCE OF 207-253.
PubMed=4327399; DOI=10.1021/bi00787a018;
Butler W.T., Ponds S.L.;
"Chemical studies on the cyanogen bromide peptides of rat skin
collagen. Amino acid sequence of alpha 1-CB4.";
Biochemistry 10:2076-2081(1971).
[8]
PROTEIN SEQUENCE OF 254-290, HYDROXYLATION AT LYS-254, AND
GLYCOSYLATION AT LYS-254.
PubMed=5411206; DOI=10.1021/bi00803a006;
Butler W.T.;
"Chemical studies on the cyanogen bromide peptides of rat skin
collagen. The covalent structure of alpha 1-CB5, the major hexose-
containing cyanogen bromide peptide of alpha 1.";
Biochemistry 9:44-50(1970).
[9]
PROTEIN SEQUENCE OF 291-389.
PubMed=4335087; DOI=10.1021/bi00800a019;
Balian G., Click E.M., Bornstein P.;
"Structure of rat skin collagen alpha 1-CB8. Amino acid sequence of
the hydroxylamine-produced fragment HA1.";
Biochemistry 10:4470-4478(1971).
[10]
PROTEIN SEQUENCE OF 390-569.
PubMed=4342027; DOI=10.1021/bi00770a020;
Balian G., Click E.M., Hermodson M.A., Bornstein P.;
"Structure of rat skin collagen alpha 1-CBB. Amino acid sequence of
the hydroxyl amine-produced fragment HA2.";
Biochemistry 11:3798-3806(1972).
[11]
PROTEIN SEQUENCE OF 570-718.
PubMed=4366532; DOI=10.1021/bi00711a025;
Butler W.T., Underwood S.P., Finch J.E. Jr.;
"Chemical studies on the cyanogen bromide peptides of rat skin
collagen. Amino acid sequence of alpha 1-CB3.";
Biochemistry 13:2946-2953(1974).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 680-718.
PubMed=6395893; DOI=10.1021/bi00320a049;
Genovese C., Rowe D., Kream B.;
"Construction of DNA sequences complementary to rat alpha 1 and alpha
2 collagen mRNA and their use in studying the regulation of type I
collagen synthesis by 1,25-dihydroxyvitamin D.";
Biochemistry 23:6210-6216(1984).
[13]
PROTEIN SEQUENCE OF 1103-1186.
PubMed=4126850; DOI=10.1111/j.1432-1033.1973.tb02987.x;
Stoltz M., Timpl R., Furthmayr H., Kuehn K.;
"Structural and immunogenic properties of a major antigenic
determinant in neutral salt-extracted rat-skin collagen.";
Eur. J. Biochem. 37:287-294(1973).
[14]
PROTEIN SEQUENCE OF 1186-1206.
PubMed=4636751; DOI=10.1016/0014-5793(72)80542-8;
Stoltz M., Timpl R., Kuehn K.;
"Non-helical regions in rat collagen alpha 1-chain.";
FEBS Lett. 26:61-65(1972).
[15]
INTERACTION WITH MRC2.
STRAIN=Sprague-Dawley;
PubMed=15817460; DOI=10.1074/jbc.M501155200;
Thomas E.K., Nakamura M., Wienke D., Isacke C.M., Pozzi A., Liang P.;
"Endo180 binds to the C-terminal region of type I collagen.";
J. Biol. Chem. 280:22596-22605(2005).
[16]
IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION.
Xiong X., Ghosh R., Hiller E., Drepper F., Knapp B., Brunner H.,
Rupp S.;
"A new procedure for rapid, high yield purification of Type I collagen
for tissue engineering.";
Process Biochem. 44:1200-1212(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-260 AND
SER-776, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[18]
X-RAY CRYSTALLOGRAPHY (5.16 ANGSTROMS) OF 152-1207.
PubMed=16751282; DOI=10.1073/pnas.0502718103;
Orgel J.P.R.O., Irving T.C., Miller A., Wess T.J.;
"Microfibrillar structure of type I collagen in situ.";
Proc. Natl. Acad. Sci. U.S.A. 103:9001-9005(2006).
-!- 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 (PubMed:15817460). Interacts with TRAM2.
Interacts with MFAP4 in a Ca (2+)-dependent manner.
{ECO:0000250|UniProtKB:P02452, ECO:0000250|UniProtKB:P02453,
ECO:0000269|PubMed:15817460}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- 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. {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.
{ECO:0000269|PubMed:5411206}.
-!- PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to
the oxygen atom of a post-translationally added hydroxyl group.
{ECO:0000269|PubMed:5411206}.
-!- PTM: Hydroxylation on proline residues within the sequence motif,
GXPG, is most likely to be 4-hydroxy as this fits the requirement
for 4-hydroxylation in vertebrates. {ECO:0000269|PubMed:5411206}.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
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EMBL; Z78279; CAB01633.1; -; mRNA.
EMBL; CH473948; EDM05727.1; -; Genomic_DNA.
EMBL; BC133728; AAI33729.1; -; mRNA.
EMBL; M11432; AAA40832.1; ALT_SEQ; mRNA.
PIR; A90559; CGRT1S.
RefSeq; NP_445756.1; NM_053304.1.
UniGene; Rn.2953; -.
PDB; 3HQV; Fiber; 5.16 A; A/C=152-1207.
PDB; 3HR2; Fiber; 5.16 A; A/C=152-1207.
PDBsum; 3HQV; -.
PDBsum; 3HR2; -.
ProteinModelPortal; P02454; -.
SMR; P02454; -.
BioGrid; 248045; 1.
DIP; DIP-36887N; -.
IntAct; P02454; 2.
STRING; 10116.ENSRNOP00000005311; -.
iPTMnet; P02454; -.
PhosphoSitePlus; P02454; -.
PaxDb; P02454; -.
PRIDE; P02454; -.
Ensembl; ENSRNOT00000005311; ENSRNOP00000005311; ENSRNOG00000003897.
GeneID; 29393; -.
KEGG; rno:29393; -.
UCSC; RGD:61817; rat.
CTD; 1277; -.
RGD; 61817; Col1a1.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00840000129673; -.
HOGENOM; HOG000085654; -.
HOVERGEN; HBG004933; -.
InParanoid; P02454; -.
KO; K06236; -.
OMA; FQFEYGS; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P02454; -.
TreeFam; TF344135; -.
Reactome; R-RNO-114604; GPVI-mediated activation cascade.
Reactome; R-RNO-1442490; Collagen degradation.
Reactome; R-RNO-1474244; Extracellular matrix organization.
Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-216083; Integrin cell surface interactions.
Reactome; R-RNO-2214320; Anchoring fibril formation.
Reactome; R-RNO-2243919; Crosslinking of collagen fibrils.
Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-RNO-3000178; ECM proteoglycans.
Reactome; R-RNO-430116; GP1b-IX-V activation signalling.
Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen.
Reactome; R-RNO-76009; Platelet Aggregation (Plug Formation).
Reactome; R-RNO-8874081; MET activates PTK2 signaling.
Reactome; R-RNO-8948216; Collagen chain trimerization.
EvolutionaryTrace; P02454; -.
PRO; PR:P02454; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000003897; -.
Genevisible; P02454; RN.
GO; GO:0005584; C:collagen type I trimer; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
GO; GO:1902618; P:cellular response to fluoride; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0071306; P:cellular response to vitamin E; IEP:RGD.
GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IDA:MGI.
GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEP:RGD.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0031960; P:response to corticosteroid; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:1902617; P:response to fluoride; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0044691; P:tooth eruption; IEP:RGD.
GO; GO:0034505; P:tooth mineralization; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IMP:RGD.
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; 12.
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;
3D-structure; Calcium; Collagen; Complete proteome;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Glycoprotein; Hydroxylation; Metal-binding; Phosphoprotein;
Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 22 {ECO:0000255}.
PROPEP 23 151 N-terminal propeptide.
{ECO:0000269|PubMed:5777344}.
/FTId=PRO_0000043358.
CHAIN 152 1207 Collagen alpha-1(I) chain.
/FTId=PRO_0000043359.
PROPEP 1208 1453 C-terminal propeptide. {ECO:0000250}.
/FTId=PRO_0000043360.
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 1176 1186 Major antigenic determinant (of neutral
salt-extracted rat skin collagen).
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:0000269|PubMed:5777344}.
MOD_RES 160 160 Allysine. {ECO:0000269|PubMed:5777344}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 179 179 4-hydroxyproline. {ECO:0000305}.
MOD_RES 182 182 4-hydroxyproline. {ECO:0000305}.
MOD_RES 185 185 4-hydroxyproline. {ECO:0000305}.
MOD_RES 194 194 4-hydroxyproline. {ECO:0000305}.
MOD_RES 197 197 4-hydroxyproline. {ECO:0000305}.
MOD_RES 200 200 4-hydroxyproline. {ECO:0000305}.
MOD_RES 254 254 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:5411206}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 575 575 5-hydroxylysine. {ECO:0000305}.
MOD_RES 698 698 5-hydroxylysine. {ECO:0000305}.
MOD_RES 776 776 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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:0000269|PubMed:5411206}.
CARBOHYD 1354 1354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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}.
CONFLICT 143 143 P -> L (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 202 202 A -> G (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 209 209 R -> P (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 232 232 E -> Q (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 268 268 D -> N (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 286 286 A -> T (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 307 307 S -> T (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 313 313 N -> D (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 421 421 N -> T (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 497 497 A -> S (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 773 773 T -> A (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 794 794 P -> A (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 958 958 E -> K (in Ref. 1; CAB01633).
{ECO:0000305}.
CONFLICT 1111 1111 S -> P (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 1163 1163 S -> A (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 1166 1166 A -> S (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 1187 1187 F -> L (in Ref. 14; AA sequence).
{ECO:0000305}.
CONFLICT 1190 1190 L -> F (in Ref. 14; AA sequence).
{ECO:0000305}.
SEQUENCE 1453 AA; 137953 MW; BCDDC40C3167AE59 CRC64;
MFSFVDLRLL LLLGATALLT HGQEDIPEVS CIHNGLRVPN GETWKPDVCL ICICHNGTAV
CDGVLCKEDL DCPNPQKREG ECCPFCPEEY VSPDAEVIGV EGPKGDPGPQ GPRGPVGPPG
QDGIPGQPGL PGPPGPPGPP GPPGLGGNFA SQMSYGYDEK SAGVSVPGPM GPSGPRGLPG
PPGAPGPQGF QGPPGEPGEP GASGPMGPRG PPGPPGKNGD DGEAGKPGRP GERGPPGPQG
ARGLPGTAGL PGMKGHRGFS GLDGAKGDTG PAGPKGEPGS PGENGAPGQM GPRGLPGERG
RPGPPGSAGA RGNDGAVGAA GPPGPTGPTG PPGFPGAAGA KGEAGPQGAR GSEGPQGVRG
EPGPPGPAGA AGPAGNPGAD GQPGAKGANG APGIAGAPGF PGARGPSGPQ GPSGAPGPKG
NSGEPGAPGN KGDTGAKGEP GPAGVQGPPG PAGEEGKRGA RGEPGPSGLP GPPGERGGPG
SRGFPGADGV AGPKGPAGER GSPGPAGPKG SPGEAGRPGE AGLPGAKGLT GSPGSPGPDG
KTGPPGPAGQ DGRPGPAGPP GARGQAGVMG FPGPKGTAGE PGKAGERGVP GPPGAVGPAG
KDGEAGAQGA PGPAGPAGER GEQGPAGSPG FQGLPGPAGP PGEAGKPGEQ GVPGDLGAPG
PSGARGERGF PGERGVQGPP GPAGPRGNNG APGNDGAKGD TGAPGAPGSQ GAPGLQGMPG
ERGAAGLPGP KGDRGDAGPK GADGSPGKDG VRGLTGPIGP PGPAGAPGDK GETGPSGPAG
PTGARGAPGD RGEPGPPGPA GFAGPPGADG QPGAKGEPGD TGVKGDAGPP GPAGPAGPPG
PIGNVGAPGP KGSRGAAGPP GATGFPGAAG RVGPPGPSGN AGPPGPPGPV GKEGGKGPRG
ETGPAGRPGE VGPPGPPGPA GEKGSPGADG PAGSPGTPGP QGIAGQRGVV GLPGQRGERG
FPGLPGPSGE PGKQGPSGAS 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
DGFQFEYGSE GSDPADVAIQ LTFLRLMSTE ASQNITYHCK NSVAYMDQQT GNLKKSLLLQ
GSNEIELRGE GNSRFTYSTL VDGCTSHTGT WGKTVIEYKT TKTSRLPIID VAPLDIGAPD
QEFGMDIGPA CFV


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Catalog number Product name Quantity
E0571h ELISA Alpha-1 type I collagen,COL1A1,Collagen alpha-1(I) chain,Homo sapiens,Human 96T
E0571m ELISA Alpha-1 type I collagen,Col1a1,Cola1,Collagen alpha-1(I) chain,Mouse,Mus musculus 96T
E0571m ELISA kit Alpha-1 type I collagen,Col1a1,Cola1,Collagen alpha-1(I) chain,Mouse,Mus musculus 96T
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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