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Collagen alpha-2(I) chain (Alpha-2 type I collagen)

 CO1A2_CHICK             Reviewed;        1363 AA.
P02467; F1P0H9; P87491; P87492; Q90758; Q90792; Q90795; Q90797;
Q92014;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 3.
23-MAY-2018, entry version 132.
RecName: Full=Collagen alpha-2(I) chain;
AltName: Full=Alpha-2 type I collagen;
Flags: Precursor;
Name=COL1A2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl {ECO:0000312|Ensembl:ENSGALP00000015687,
ECO:0000312|Proteomes:UP000000539};
PubMed=15592404; DOI=10.1038/nature03154;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-245; 263-449 AND 467-1363.
PubMed=3868961; DOI=10.1111/j.1749-6632.1985.tb51159.x;
Boedtker H., Finer M., Aho S.;
"The structure of the chicken alpha 2 collagen gene.";
Ann. N. Y. Acad. Sci. 460:85-116(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
PubMed=6135195; DOI=10.1093/nar/11.1.91;
Tate V.E., Finer M.H., Boedtker H., Doty P.;
"Chick pro alpha 2 (I) collagen gene: exon location and coding
potential for the prepropeptide.";
Nucleic Acids Res. 11:91-104(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
PubMed=6946474; DOI=10.1073/pnas.78.9.5334;
Vogeli G., Ohkubo H., Sobel M.E., Yamada Y., Pastan I.,
de Crombrugghe B.;
"Structure of the promoter for chicken alpha 2 type I collagen gene.";
Proc. Natl. Acad. Sci. U.S.A. 78:5334-5338(1981).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
PubMed=6473103; DOI=10.1093/nar/12.15.6117;
Aho S., Tate V.E., Boedtker H.;
"Location of the 11 bp exon in the chicken pro alpha 2(I) collagen
gene.";
Nucleic Acids Res. 12:6117-6125(1984).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
PubMed=3678834; DOI=10.1016/0378-1119(87)90159-4;
Finer M.H., Boedtker H., Doty P.;
"Construction and characterization of cDNA clones encoding the 5' end
of the chicken pro alpha 1(I) collagen mRNA.";
Gene 56:71-78(1987).
[7]
PROTEIN SEQUENCE OF 74-92; 264-449 AND 1089-1171.
PubMed=5443712; DOI=10.1016/0006-291X(70)90638-8;
Vuust J., Lane J.M., Fietzek P.P., Miller E.J., Piez K.A.;
"The order of the CNBr peptides from the alpha 2 chain of collagen.";
Biochem. Biophys. Res. Commun. 38:703-708(1970).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-91; 264-449 AND 1089-1170.
PubMed=6272119; DOI=10.1038/294129a0;
Wozney J., Hanahan D., Tate V.E., Boedtker H., Doty P.;
"Structure of the pro alpha 2 (I) collagen gene.";
Nature 294:129-135(1981).
[9]
PROTEIN SEQUENCE OF 78-92, ALLYSINE AT LYS-83, AND PYROGLUTAMATE
FORMATION AT GLN-78.
TISSUE=Skin;
PubMed=4313735; DOI=10.1021/bi00806a012;
Kang A.H., Gross J.;
"Amino acid sequence of cyanogen bromide peptides from the amino-
terminal region of chick skicollagen.";
Biochemistry 9:796-804(1970).
[10]
PROTEIN SEQUENCE OF 78-92 AND 416-449, AND PYROGLUTAMATE FORMATION AT
GLN-78.
TISSUE=Skin;
PubMed=5809220; DOI=10.1021/bi00836a011;
Kang A.H., Igarashi S., Gross J.;
"Characterization of the cyanogen bromide peptides from the alpha-2
chain of chick skin collagen.";
Biochemistry 8:3200-3204(1969).
[11]
PROTEIN SEQUENCE OF 78-92 AND 416-449, AND PYROGLUTAMATE FORMATION AT
GLN-78.
TISSUE=Bone;
PubMed=5785233; DOI=10.1021/bi00833a053;
Lane J.M., Miller E.J.;
"Isolation and characterization of the peptides derived from the alpha
2 chain of chick bone collagen after cyanogen bromide cleavage.";
Biochemistry 8:2134-2139(1969).
[12]
PROTEIN SEQUENCE OF 78-95 AND 416-446.
PubMed=5443711; DOI=10.1016/0006-291X(70)90637-6;
Igarashi S., Kang A.H., Gross J.;
"Renaturation and ordering by electron microscopy of the cyanogen
bromide peptides from the alpha 2 chain of chick skin collagen.";
Biochem. Biophys. Res. Commun. 38:697-702(1970).
[13]
PROTEIN SEQUENCE OF 417-445, AND HYDROXYLATION AT PRO-440 AND PRO-443.
TISSUE=Skin;
PubMed=5544653; DOI=10.1021/bi00780a010;
Highberger J.H., Kang A.H., Gross J.;
"Comparative studies on the amino acid sequence of the alpha 2-CB2
peptides from chick and rat skin collagens.";
Biochemistry 10:610-616(1971).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 567-588.
PubMed=364479; DOI=10.1073/pnas.75.11.5417;
Lehrach H., Frischauf A.-M., Hanahan D., Wozney J., Fuller F.,
Crkvenjakov R., Boedtker H., Doty P.;
"Construction and characterization of a 2.5-kilobase procollagen
clone.";
Proc. Natl. Acad. Sci. U.S.A. 75:5417-5421(1978).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 903-1363.
PubMed=6927845; DOI=10.1021/bi00507a054;
Fuller F., Boedtker H.;
"Sequence determination and analysis of the 3' region of chicken pro-
alpha 1(I) and pro-alpha 2(I) collagen messenger ribonucleic acids
including the carboxy-terminal propeptide sequences.";
Biochemistry 20:996-1006(1981).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 999-1170 AND 1235-1363.
PubMed=6267043;
Dickson L.A., Ninomiya Y., Bernard M.P., Pesciotta D.M., Parsons J.,
Green G., Eikenberry E.F., de Crombrugghe B., Vogeli G., Pastan I.,
Fietzek P.P., Olsen B.R.;
"The exon/intron structure of the 3'-region of the pro alpha 2(I)
collagen gene.";
J. Biol. Chem. 256:8407-8415(1981).
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 933-955 AND 969-981.
PubMed=6159982; DOI=10.1016/0092-8674(80)90432-8;
Avvedimento V.E., Vogeli G., Yamada Y., Maizel J.V. Jr., Pastan I.,
de Crombrugghe B.;
"Correlation between splicing sites within an intron and their
sequence complementarity with U1 RNA.";
Cell 21:689-696(1980).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-161; 468-518 AND 927-955.
PubMed=7460017; DOI=10.1016/0092-8674(80)90565-6;
Yamada Y., Avvedimento V.E., Mudryj M., Ohkubo H., Vogeli G.,
Irani M., Pastan I., de Crombrugghe B.;
"The collagen gene: evidence for its evolutionary assembly by
amplification of a DNA segment containing an exon of 54 bp.";
Cell 22:887-892(1980).
-!- 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.
-!- 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: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:5544653}.
-!- PTM: The N-terminus of the mature protein is blocked.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
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EMBL; AADN04000096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M25963; AAA69960.1; -; Genomic_DNA.
EMBL; M25956; AAA69960.1; JOINED; Genomic_DNA.
EMBL; M25959; AAA69960.1; JOINED; Genomic_DNA.
EMBL; M25961; AAA69960.1; JOINED; Genomic_DNA.
EMBL; M25962; AAA69960.1; JOINED; Genomic_DNA.
EMBL; M25965; AAA69961.1; -; Genomic_DNA.
EMBL; M25964; AAA69961.1; JOINED; Genomic_DNA.
EMBL; M25984; AAA69962.1; -; Genomic_DNA.
EMBL; M25957; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25966; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25967; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25969; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25970; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25971; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25972; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25973; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25974; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25976; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25977; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25978; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25979; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25980; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25981; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25982; AAA69962.1; JOINED; Genomic_DNA.
EMBL; M25983; AAA69962.1; JOINED; Genomic_DNA.
EMBL; J00826; AAA51611.1; -; Genomic_DNA.
EMBL; J00821; AAA51611.1; JOINED; Genomic_DNA.
EMBL; K00792; AAA51611.1; JOINED; Genomic_DNA.
EMBL; J00830; AAA51613.1; -; Genomic_DNA.
EMBL; J00829; AAA51613.1; JOINED; Genomic_DNA.
EMBL; J00837; AAA51614.1; -; Genomic_DNA.
EMBL; J00812; AAA51615.1; -; Genomic_DNA.
EMBL; J00811; AAA51615.1; JOINED; Genomic_DNA.
EMBL; J00814; AAA51615.1; JOINED; Genomic_DNA.
EMBL; J00815; AAA51615.1; JOINED; Genomic_DNA.
EMBL; X02657; CAA26493.1; -; mRNA.
EMBL; K00794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; V00390; CAA23688.1; -; mRNA.
EMBL; M17608; AAA48673.1; -; mRNA.
EMBL; M10581; AAA48637.1; -; Genomic_DNA.
EMBL; M10540; AAA48638.1; -; Genomic_DNA.
EMBL; J00828; AAA51612.1; -; Genomic_DNA.
EMBL; J00827; AAA51612.1; JOINED; Genomic_DNA.
EMBL; J00832; AAD22117.1; -; Genomic_DNA.
EMBL; J00831; AAD22117.1; JOINED; Genomic_DNA.
EMBL; J00833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; J00822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; I50173; I50173.
PIR; I50206; CGCH2S.
PIR; S10847; S10847.
UniGene; Gga.5097; -.
SMR; P02467; -.
STRING; 9031.ENSGALP00000015687; -.
PaxDb; P02467; -.
PRIDE; P02467; -.
Ensembl; ENSGALT00000015703; ENSGALP00000015687; ENSGALG00000009641.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00900000140789; -.
HOVERGEN; HBG004933; -.
InParanoid; P02467; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P02467; -.
TreeFam; TF344135; -.
Reactome; R-GGA-1442490; Collagen degradation.
Reactome; R-GGA-1474244; Extracellular matrix organization.
Reactome; R-GGA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-GGA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-GGA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-GGA-216083; Integrin cell surface interactions.
Reactome; R-GGA-2243919; Crosslinking of collagen fibrils.
Reactome; R-GGA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-GGA-3000178; ECM proteoglycans.
Reactome; R-GGA-430116; GP1b-IX-V activation signalling.
Reactome; R-GGA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-GGA-76009; Platelet Aggregation (Plug Formation).
Reactome; R-GGA-8874081; MET activates PTK2 signaling.
Reactome; R-GGA-8948216; Collagen chain trimerization.
PMAP-CutDB; P02467; -.
Proteomes; UP000000539; Chromosome 2.
Bgee; ENSGALG00000009641; -.
GO; GO:0005584; C:collagen type I trimer; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005583; C:fibrillar collagen trimer; IDA:AgBase.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
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:0030674; F:protein binding, bridging; IEA:Ensembl.
GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 5.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
PROSITE; PS51461; NC1_FIB; 1.
1: Evidence at protein level;
Calcium; Collagen; Complete proteome; Direct protein sequencing;
Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
Metal-binding; Pyrrolidone carboxylic acid; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 22 {ECO:0000250|UniProtKB:P02466}.
PROPEP 23 77 N-terminal propeptide.
{ECO:0000250|UniProtKB:P08123}.
/FTId=PRO_0000005815.
CHAIN 78 1117 Collagen alpha-2(I) chain.
/FTId=PRO_0000005816.
PROPEP 1118 1363 C-terminal propeptide.
{ECO:0000250|UniProtKB:P08123}.
/FTId=PRO_0000005817.
DOMAIN 1128 1363 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
METAL 1176 1176 Calcium. {ECO:0000250|UniProtKB:Q03692}.
METAL 1178 1178 Calcium. {ECO:0000250|UniProtKB:Q03692}.
METAL 1179 1179 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q03692}.
METAL 1181 1181 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q03692}.
METAL 1184 1184 Calcium. {ECO:0000250|UniProtKB:Q03692}.
MOD_RES 23 23 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P08123}.
MOD_RES 78 78 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:4313735,
ECO:0000305|PubMed:5785233,
ECO:0000305|PubMed:5809220}.
MOD_RES 83 83 Allysine. {ECO:0000269|PubMed:4313735}.
MOD_RES 176 176 5-hydroxylysine; alternate.
{ECO:0000250|UniProtKB:P08123}.
MOD_RES 440 440 4-hydroxyproline.
{ECO:0000269|PubMed:5544653}.
MOD_RES 443 443 4-hydroxyproline.
{ECO:0000269|PubMed:5544653}.
CARBOHYD 176 176 O-linked (Gal...) hydroxylysine;
alternate.
{ECO:0000250|UniProtKB:P08123}.
CARBOHYD 1264 1264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1158 1190 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1198 1361 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1269 1314 {ECO:0000255|PROSITE-ProRule:PRU00793}.
CONFLICT 428 430 VGA -> AGV (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 974 974 P -> L (in Ref. 17; AAA48638).
{ECO:0000305}.
CONFLICT 1010 1010 P -> H (in Ref. 16; AAA51615).
{ECO:0000305}.
CONFLICT 1055 1055 P -> H (in Ref. 16; AAA51615).
{ECO:0000305}.
CONFLICT 1061 1061 P -> H (in Ref. 16; AAA51615).
{ECO:0000305}.
CONFLICT 1262 1262 S -> P (in Ref. 16; AAA51615).
{ECO:0000305}.
SEQUENCE 1363 AA; 128995 MW; 41FFEE5077B428B4 CRC64;
MLSFVDTRIL LLLAVTSYLA TSQHLFQASA GRKGPRGDKG PQGERGPPGP PGRDGEDGPP
GPPGPPGPPG LGGNFAAQYD PSKAADFGPG PMGLMGPRGP PGASGPPGPP GFQGVPGEPG
EPGQTGPQGP RGPPGPPGKA GEDGHPGKPG RPGERGVAGP QGARGFPGTP GLPGFKGIRG
HNGLDGQKGQ PGTPGTKGEP GAPGENGTPG QPGARGLPGE RGRIGAPGPA GARGSDGSAG
PTGPAGPIGA AGPPGFPGAP GAKGEIGPAG NVGPTGPAGP RGEIGLPGSS GPVGPPGNPG
ANGLPGAKGA AGLPGVAGAP GLPGPRGIPG PPGPAGPSGA RGLVGEPGPA GAKGESGNKG
EPGAAGPPGP PGPSGEEGKR GSNGEPGSAG PPGPAGLRGV PGSRGLPGAD GRAGVMGPAG
NRGASGPVGA KGPNGDAGRP GEPGLMGPRG LPGQPGSPGP AGKEGPVGFP GADGRVGPIG
PAGNRGEPGN IGFPGPKGPT GEPGKPGEKG NVGLAGPRGA PGPEGNNGAQ GPPGVTGNQG
AKGETGPAGP PGFQGLPGPS GPAGEAGKPG ERGLHGEFGV PGPAGPRGER GLPGESGAVG
PAGPIGSRGP SGPPGPDGNK GEPGNVGPAG APGPAGPGGI PGERGVAGVP GGKGEKGAPG
LRGDTGATGR DGARGLPGAI GAPGPAGGAG DRGEGGPAGP AGPAGARGIP GERGEPGPVG
PSGFAGPPGA AGQPGAKGER GPKGPKGETG PTGAIGPIGA SGPPGPVGAA GPAGPRGDAG
PPGMTGFPGA AGRVGPPGPA GITGPPGPPG PAGKDGPRGL RGDVGPVGRT GEQGIAGPPG
FAGEKGPSGE AGAAGPPGTP GPQGILGAPG ILGLPGSRGE RGLPGIAGAT GEPGPLGVSG
PPGARGPSGP VGSPGPNGAP GEAGRDGNPG NDGPPGRDGA PGFKGERGAP GNPGPSGALG
APGPHGQVGP SGKPGNRGDP GPVGPVGPAG AFGPRGLAGP QGPRGEKGEP GDKGHRGLPG
LKGHNGLQGL PGLAGQHGDQ GPPGNNGPAG PRGPPGPSGP PGKDGRNGLP GPIGPAGVRG
SHGSQGPAGP PGPPGPPGPP GPNGGGYEVG FDAEYYRADQ PSLRPKDYEV DATLKTLNNQ
IETLLTPEGS KKNPARTCRD LRLSHPEWSS GFYWIDPNQG CTADAIRAYC DFATGETCIH
ASLEDIPTKT WYVSKNPKDK KHIWFGETIN GGTQFEYNGE GVTTKDMATQ LAFMRLLANH
ASQNITYHCK NSIAYMDEET GNLKKAVILQ GSNDVELRAE GNSRFTFSVL VDGCSKKNNK
WGKTIIEYRT NKPSRLPILD IAPLDIGGAD QEFGLHIGPV CFK


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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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