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Interstitial collagenase (EC 3.4.24.7) (Fibroblast collagenase) (Matrix metalloproteinase-1) (MMP-1) [Cleaved into: 22 kDa interstitial collagenase; 27 kDa interstitial collagenase]

 MMP1_HUMAN              Reviewed;         469 AA.
P03956; P08156;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 3.
12-SEP-2018, entry version 211.
RecName: Full=Interstitial collagenase;
EC=3.4.24.7 {ECO:0000269|PubMed:1645757, ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297, ECO:0000269|PubMed:2557822};
AltName: Full=Fibroblast collagenase;
AltName: Full=Matrix metalloproteinase-1;
Short=MMP-1;
Contains:
RecName: Full=22 kDa interstitial collagenase;
Contains:
RecName: Full=27 kDa interstitial collagenase;
Flags: Precursor;
Name=MMP1; Synonyms=CLG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=2167156;
Templeton N.S., Brown P.D., Levy A.T., Margulies I.M.K., Liotta L.A.,
Stetler-Stevenson W.G.;
"Cloning and characterization of human tumor cell interstitial
collagenase.";
Cancer Res. 50:5431-5437(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3030290; DOI=10.1042/bj2400913;
Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A.,
Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.;
"Comparison of human stromelysin and collagenase by cloning and
sequence analysis.";
Biochem. J. 240:913-916(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3009463;
Goldberg G.I., Wilhelm S.M., Kronberger A., Bauer E.A., Grant G.A.,
Eisen A.Z.;
"Human fibroblast collagenase. Complete primary structure and homology
to an oncogene transformation-induced rat protein.";
J. Biol. Chem. 261:6600-6605(1986).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lin D., Duncan M., Allen E., Araujo R., Aparicio A., Chai A.,
Chung E., Davis K., Federspiel N., Hyman R., Kalman S., Komp C.,
Kurdi O., Lashkari D., Lew H., Namath A., Oefner P., Roberts D.,
Heller R., Davis R.W.;
"Three matrix metalloproteinases on 81kb of P1 insert.";
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[5]
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-191; GLN-405 AND
THR-406.
NIEHS SNPs program;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
PubMed=3037355; DOI=10.1128/MCB.7.6.2256;
Angel P., Baumann I., Stein B., Delius H., Rahmsdorf H.J.,
Herrlich P.;
"12-O-tetradecanoyl-phorbol-13-acetate induction of the human
collagenase gene is mediated by an inducible enhancer element located
in the 5'-flanking region.";
Mol. Cell. Biol. 7:2256-2266(1987).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-70.
TISSUE=Synovial cell;
PubMed=3027129; DOI=10.1172/JCI112845;
Brinckerhoff C.E., Ruby P.L., Austin S.D., Fini M.E., White H.D.;
"Molecular cloning of human synovial cell collagenase and selection of
a single gene from genomic DNA.";
J. Clin. Invest. 79:542-546(1987).
[10]
PROTEIN SEQUENCE OF 100-112 AND 270-287, AND CATALYTIC ACTIVITY.
TISSUE=Fibroblast;
PubMed=2557822; DOI=10.1042/bj2630201;
Clark I.M., Cawston T.E.;
"Fragments of human fibroblast collagenase. Purification and
characterization.";
Biochem. J. 263:201-206(1989).
[11]
SIMILARITY TO THERMOLYSIN TYPE PROTEASES.
PubMed=3032950;
McKerrow J.H.;
"Human fibroblast collagenase contains an amino acid sequence
homologous to the zinc-binding site of Serratia protease.";
J. Biol. Chem. 262:5943-5943(1987).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
PubMed=2153297; DOI=10.1073/pnas.87.1.364;
Springman E.B., Angleton E.L., Birkedal-Hansen H., Van Wart H.E.;
"Multiple modes of activation of latent human fibroblast collagenase:
evidence for the role of a Cys73 active-site zinc complex in latency
and a 'cysteine switch' mechanism for activation.";
Proc. Natl. Acad. Sci. U.S.A. 87:364-368(1990).
[13]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=1645757; DOI=10.1172/JCI115262;
Desrochers P.E., Jeffrey J.J., Weiss S.J.;
"Interstitial collagenase (matrix metalloproteinase-1) expresses
serpinase activity.";
J. Clin. Invest. 87:2258-2265(1991).
[14]
GLYCOSYLATION AT ASN-120.
PubMed=10092871; DOI=10.1046/j.1432-1327.1999.00105.x;
Saarinen J., Welgus H.G., Flizar C.A., Kalkkinen N., Helin J.;
"N-glycan structures of matrix metalloproteinase-1 derived from human
fibroblasts and from HT-1080 fibrosarcoma cells.";
Eur. J. Biochem. 259:829-840(1999).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH HIV-1 TAT
(MICROBIAL INFECTION).
PubMed=16807369; DOI=10.1096/fj.05-5619fje;
Rumbaugh J., Turchan-Cholewo J., Galey D., St Hillaire C.,
Anderson C., Conant K., Nath A.;
"Interaction of HIV Tat and matrix metalloproteinase in HIV
neuropathogenesis: a new host defense mechanism.";
FASEB J. 20:1736-1738(2006).
[16]
PHOSPHORYLATION AT SER-57; THR-274 AND TYR-360, AND MUTAGENESIS OF
TYR-360.
PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L.,
Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.;
"A secreted tyrosine kinase acts in the extracellular environment.";
Cell 158:1033-1044(2014).
[17]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 101-269 IN COMPLEX WITH
CALCIUM AND ZINC.
PubMed=7656013; DOI=10.1038/nsb0294-106;
Borkakoti N., Winkler F.K., Williams D.H., D'Arcy A., Broadhurst M.J.,
Brown P.A., Johnson W.H., Murray E.J.;
"Structure of the catalytic domain of human fibroblast collagenase
complexed with an inhibitor.";
Nat. Struct. Biol. 1:106-110(1994).
[18]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 102-269 IN COMPLEX WITH
CALCIUM AND ZINC.
PubMed=8031754; DOI=10.1021/bi00193a006;
Lovejoy B., Hassell A.M., Luther M.A., Weigl D., Jordan S.R.;
"Crystal structures of recombinant 19-kDa human fibroblast collagenase
complexed to itself.";
Biochemistry 33:8207-8217(1994).
[19]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 101-269 IN COMPLEX WITH
CALCIUM AND ZINC.
PubMed=8278810; DOI=10.1126/science.8278810;
Lovejoy B., Cleasby A., Hassell A.M., Longley K., Luther M.A.,
Weigl D., McGeehan G., McElroy A.B., Drewry D., Lambert M.H.,
Jordan S.R.;
"Structure of the catalytic domain of fibroblast collagenase complexed
with an inhibitor.";
Science 263:375-377(1994).
[20]
X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 101-269 IN COMPLEX WITH
CALCIUM AND ZINC.
PubMed=8090713; DOI=10.1002/prot.340190203;
Spurlino J.C., Smallwood A.M., Carlton D.D., Banks T.M., Vavra K.J.,
Johnson J.S., Cook E.R., Falvo J., Wahl R.C., Pulvino T.A., Et A.L.;
"1.56-A structure of mature truncated human fibroblast collagenase.";
Proteins 19:98-109(1994).
[21]
STRUCTURE BY NMR OF 101-269 IN COMPLEX WITH CALCIUM AND ZINC.
PubMed=9484219; DOI=10.1021/bi972181w;
Moy F.J., Chanda P.K., Cosmi S., Pisano M.R., Urbano C., Wilhelm J.,
Powers R.;
"High-resolution solution structure of the inhibitor-free catalytic
fragment of human fibroblast collagenase determined by
multidimensional NMR.";
Biochemistry 37:1495-1504(1998).
[22]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-469 IN COMPLEX WITH
CALCIUM AND ZINC, AND DOMAIN.
PubMed=15611040; DOI=10.1074/jbc.M411084200;
Jozic D., Bourenkov G., Lim N.H., Visse R., Nagase H., Bode W.,
Maskos K.;
"X-ray structure of human proMMP-1: new insights into procollagenase
activation and collagen binding.";
J. Biol. Chem. 280:9578-9585(2005).
-!- FUNCTION: Cleaves collagens of types I, II, and III at one site in
the helical domain. Also cleaves collagens of types VII and X
(PubMed:2557822, PubMed:2153297, PubMed:1645757). In case of HIV
infection, interacts and cleaves the secreted viral Tat protein,
leading to a decrease in neuronal Tat's mediated neurotoxicity
(PubMed:16807369). {ECO:0000269|PubMed:1645757,
ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297,
ECO:0000269|PubMed:2557822}.
-!- CATALYTIC ACTIVITY: Cleavage of the triple helix of collagen at
about three-quarters of the length of the molecule from the N-
terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves
synthetic substrates and alpha-macroglobulins at bonds where P1'
is a hydrophobic residue. {ECO:0000269|PubMed:1645757,
ECO:0000269|PubMed:16807369, ECO:0000269|PubMed:2153297,
ECO:0000269|PubMed:2557822}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219};
Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219};
-!- ACTIVITY REGULATION: Can be activated without removal of the
activation peptide.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat.
{ECO:0000269|PubMed:16807369}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305|PubMed:2167156}.
-!- DOMAIN: There are two distinct domains in this protein; the
catalytic N-terminal, and the C-terminal which is involved in
substrate specificity and in binding TIMP (tissue inhibitor of
metalloproteinases).
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
{ECO:0000269|PubMed:15611040, ECO:0000269|PubMed:2153297}.
-!- PTM: Undergoes autolytic cleavage to two major forms (22 kDa and
27 kDa). A minor form (25 kDa) is the glycosylated form of the 22
kDa form. The 27 kDa form has no activity while the 22/25 kDa form
can act as activator for collagenase.
{ECO:0000269|PubMed:10092871}.
-!- PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK.
{ECO:0000269|PubMed:25171405}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Collagenase entry;
URL="https://en.wikipedia.org/wiki/Collagenase";
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EMBL; X54925; CAA38691.1; -; mRNA.
EMBL; X05231; CAA28858.1; -; mRNA.
EMBL; M13509; AAA35699.1; -; mRNA.
EMBL; U78045; AAB36941.1; -; Genomic_DNA.
EMBL; BT006874; AAP35520.1; -; mRNA.
EMBL; AY769434; AAV28732.1; -; Genomic_DNA.
EMBL; BC013875; AAH13875.1; -; mRNA.
EMBL; M16567; AAA52033.1; -; Genomic_DNA.
EMBL; M15996; AAA35700.1; -; mRNA.
CCDS; CCDS8322.1; -.
PIR; A37308; KCHUI.
RefSeq; NP_002412.1; NM_002421.3.
UniGene; Hs.83169; -.
PDB; 1AYK; NMR; -; A=101-269.
PDB; 1CGE; X-ray; 1.90 A; A=102-269.
PDB; 1CGF; X-ray; 2.10 A; A/B=102-263.
PDB; 1CGL; X-ray; 2.40 A; A/B=101-269.
PDB; 1HFC; X-ray; 1.50 A; A=101-269.
PDB; 1SU3; X-ray; 2.20 A; A/B=20-469.
PDB; 2AYK; NMR; -; A=101-269.
PDB; 2CLT; X-ray; 2.67 A; A/B=100-466.
PDB; 2J0T; X-ray; 2.54 A; A/B/C=101-269.
PDB; 2TCL; X-ray; 2.20 A; A=101-269.
PDB; 3AYK; NMR; -; A=101-269.
PDB; 3SHI; X-ray; 2.20 A; A/G/M=106-261.
PDB; 4AUO; X-ray; 3.00 A; A/B=100-466.
PDB; 4AYK; NMR; -; A=101-269.
PDB; 966C; X-ray; 1.90 A; A=108-264.
PDBsum; 1AYK; -.
PDBsum; 1CGE; -.
PDBsum; 1CGF; -.
PDBsum; 1CGL; -.
PDBsum; 1HFC; -.
PDBsum; 1SU3; -.
PDBsum; 2AYK; -.
PDBsum; 2CLT; -.
PDBsum; 2J0T; -.
PDBsum; 2TCL; -.
PDBsum; 3AYK; -.
PDBsum; 3SHI; -.
PDBsum; 4AUO; -.
PDBsum; 4AYK; -.
PDBsum; 966C; -.
ProteinModelPortal; P03956; -.
SMR; P03956; -.
BioGrid; 110456; 6.
DIP; DIP-529N; -.
IntAct; P03956; 2.
STRING; 9606.ENSP00000322788; -.
BindingDB; P03956; -.
ChEMBL; CHEMBL332; -.
DrugBank; DB08482; [[1-[N-HYDROXY-ACETAMIDYL]-3-METHYL-BUTYL]-CARBONYL-LEUCINYL]-ALANINE ETHYL ESTER.
DrugBank; DB00786; Marimastat.
DrugBank; DB08403; METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID.
DrugBank; DB07926; N-[3-(N'-HYDROXYCARBOXAMIDO)-2-(2-METHYLPROPYL)-PROPANOYL]-O-TYROSINE-N-METHYLAMIDE.
DrugBank; DB07556; N-HYDROXY-2(R)-[[(4-METHOXYPHENYL)SULFONYL](3-PICOLYL)AMINO]-3-METHYLBUTANAMIDE HYDROCHLORIDE.
DrugBank; DB08491; N-HYDROXY-2-[4-(4-PHENOXY-BENZENESULFONYL)-TETRAHYDRO-PYRAN-4-YL]-ACETAMIDE.
GuidetoPHARMACOLOGY; 1628; -.
MEROPS; M10.001; -.
GlyConnect; 301; -.
iPTMnet; P03956; -.
PhosphoSitePlus; P03956; -.
UniCarbKB; P03956; -.
BioMuta; MMP1; -.
DMDM; 116852; -.
PaxDb; P03956; -.
PeptideAtlas; P03956; -.
PRIDE; P03956; -.
ProteomicsDB; 51623; -.
DNASU; 4312; -.
Ensembl; ENST00000315274; ENSP00000322788; ENSG00000196611.
GeneID; 4312; -.
KEGG; hsa:4312; -.
UCSC; uc001phi.3; human.
CTD; 4312; -.
DisGeNET; 4312; -.
EuPathDB; HostDB:ENSG00000196611.4; -.
GeneCards; MMP1; -.
H-InvDB; HIX0201751; -.
HGNC; HGNC:7155; MMP1.
HPA; HPA004920; -.
MalaCards; MMP1; -.
MIM; 120353; gene.
neXtProt; NX_P03956; -.
OpenTargets; ENSG00000196611; -.
Orphanet; 79408; Severe generalized recessive dystrophic epidermolysis bullosa.
PharmGKB; PA30867; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P03956; -.
KO; K01388; -.
OMA; FHGTRQY; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P03956; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.7; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
SIGNOR; P03956; -.
EvolutionaryTrace; P03956; -.
GeneWiki; MMP1; -.
GenomeRNAi; 4312; -.
PMAP-CutDB; P03956; -.
PRO; PR:P03956; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000196611; Expressed in 121 organ(s), highest expression level in smooth muscle tissue.
CleanEx; HS_MMP1; -.
Genevisible; P03956; HS.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0004175; F:endopeptidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Calcium; Collagen degradation;
Complete proteome; Direct protein sequencing; Disulfide bond;
Extracellular matrix; Glycoprotein; Host-virus interaction; Hydrolase;
Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism;
Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 19
PROPEP 20 99 Activation peptide.
{ECO:0000269|PubMed:2557822}.
/FTId=PRO_0000028703.
CHAIN 100 469 Interstitial collagenase.
/FTId=PRO_0000028704.
CHAIN 100 269 22 kDa interstitial collagenase.
/FTId=PRO_0000028705.
CHAIN 270 469 27 kDa interstitial collagenase.
/FTId=PRO_0000028706.
REPEAT 275 324 Hemopexin 1.
REPEAT 325 371 Hemopexin 2.
REPEAT 374 422 Hemopexin 3.
REPEAT 423 466 Hemopexin 4.
REGION 98 276 Metalloprotease.
MOTIF 90 97 Cysteine switch.
{ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:2153297}.
ACT_SITE 219 219
METAL 92 92 Zinc 2; in inhibited form.
{ECO:0000244|PDB:1SU3,
ECO:0000269|PubMed:15611040}.
METAL 124 124 Calcium 1. {ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:8031754}.
METAL 158 158 Calcium 2. {ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754}.
METAL 168 168 Zinc 1. {ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 170 170 Zinc 1. {ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 175 175 Calcium 3. {ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810}.
METAL 176 176 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 178 178 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 180 180 Calcium 3; via carbonyl oxygen.
{ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 183 183 Zinc 1. {ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 190 190 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754}.
METAL 192 192 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754}.
METAL 194 194 Calcium 2. {ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754}.
METAL 196 196 Zinc 1. {ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 198 198 Calcium 3. {ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810}.
METAL 199 199 Calcium 1. {ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:8031754}.
METAL 201 201 Calcium 3. {ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 218 218 Zinc 2; catalytic. {ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 222 222 Zinc 2; catalytic. {ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 228 228 Zinc 2; catalytic. {ECO:0000244|PDB:1AYK,
ECO:0000244|PDB:1CGE,
ECO:0000244|PDB:1CGF,
ECO:0000244|PDB:1CGL,
ECO:0000244|PDB:1HFC,
ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2AYK,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:2J0T,
ECO:0000244|PDB:2TCL,
ECO:0000244|PDB:3AYK,
ECO:0000244|PDB:3SHI,
ECO:0000244|PDB:4AUO,
ECO:0000244|PDB:4AYK,
ECO:0000244|PDB:966C,
ECO:0000269|PubMed:15611040,
ECO:0000269|PubMed:7656013,
ECO:0000269|PubMed:8031754,
ECO:0000269|PubMed:8090713,
ECO:0000269|PubMed:8278810,
ECO:0000269|PubMed:9484219}.
METAL 285 285 Calcium 4; via carbonyl oxygen.
{ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:4AUO,
ECO:0000269|PubMed:15611040}.
METAL 329 329 Calcium 4; via carbonyl oxygen.
{ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:4AUO,
ECO:0000269|PubMed:15611040}.
METAL 378 378 Calcium 4; via carbonyl oxygen.
{ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:4AUO,
ECO:0000269|PubMed:15611040}.
METAL 427 427 Calcium 4; via carbonyl oxygen.
{ECO:0000244|PDB:1SU3,
ECO:0000244|PDB:2CLT,
ECO:0000244|PDB:4AUO,
ECO:0000269|PubMed:15611040}.
SITE 143 143 Not glycosylated.
{ECO:0000269|PubMed:10092871}.
SITE 269 270 Cleavage; by autolysis.
{ECO:0000269|PubMed:2557822}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000269|PubMed:25171405}.
MOD_RES 274 274 Phosphothreonine.
{ECO:0000269|PubMed:25171405}.
MOD_RES 360 360 Phosphotyrosine; by PKDCC.
{ECO:0000269|PubMed:25171405}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10092871}.
/FTId=CAR_000105.
DISULFID 278 466 {ECO:0000250}.
VARIANT 29 29 Q -> P (in dbSNP:rs554499).
/FTId=VAR_011969.
VARIANT 191 191 I -> V (in dbSNP:rs17879973).
{ECO:0000269|Ref.6}.
/FTId=VAR_021024.
VARIANT 252 252 D -> G (in dbSNP:rs513964).
/FTId=VAR_011970.
VARIANT 262 262 R -> S (in dbSNP:rs12282811).
/FTId=VAR_054005.
VARIANT 405 405 R -> Q (in dbSNP:rs17879165).
{ECO:0000269|Ref.6}.
/FTId=VAR_021025.
VARIANT 406 406 S -> T (in dbSNP:rs17884120).
{ECO:0000269|Ref.6}.
/FTId=VAR_021026.
MUTAGEN 360 360 Y->F: Partial reduction of tyrosine
phosphorylation in the presence of
PKDCC/VLK. {ECO:0000269|PubMed:25171405}.
CONFLICT 43 43 N -> K (in Ref. 9; AAA35700).
{ECO:0000305}.
CONFLICT 64 64 Missing (in Ref. 9; AAA35700).
{ECO:0000305}.
CONFLICT 115 115 T -> R (in Ref. 3; AAA35699).
{ECO:0000305}.
CONFLICT 200 200 D -> H (in Ref. 2; CAA28858).
{ECO:0000305}.
CONFLICT 208 208 R -> T (in Ref. 2; CAA28858).
{ECO:0000305}.
CONFLICT 317 317 I -> T (in Ref. 2; CAA28858).
{ECO:0000305}.
CONFLICT 410 410 G -> S (in Ref. 3; AAA35699).
{ECO:0000305}.
HELIX 33 41 {ECO:0000244|PDB:1SU3}.
HELIX 59 70 {ECO:0000244|PDB:1SU3}.
HELIX 81 87 {ECO:0000244|PDB:1SU3}.
STRAND 103 106 {ECO:0000244|PDB:1AYK}.
STRAND 112 118 {ECO:0000244|PDB:1HFC}.
STRAND 123 125 {ECO:0000244|PDB:3SHI}.
HELIX 127 142 {ECO:0000244|PDB:1HFC}.
STRAND 144 146 {ECO:0000244|PDB:2J0T}.
STRAND 148 151 {ECO:0000244|PDB:1HFC}.
STRAND 153 155 {ECO:0000244|PDB:1HFC}.
STRAND 158 164 {ECO:0000244|PDB:1HFC}.
STRAND 169 171 {ECO:0000244|PDB:1HFC}.
STRAND 176 179 {ECO:0000244|PDB:1HFC}.
STRAND 182 184 {ECO:0000244|PDB:1HFC}.
STRAND 187 189 {ECO:0000244|PDB:1HFC}.
TURN 190 193 {ECO:0000244|PDB:1HFC}.
STRAND 195 198 {ECO:0000244|PDB:1HFC}.
STRAND 204 209 {ECO:0000244|PDB:1HFC}.
HELIX 212 223 {ECO:0000244|PDB:1HFC}.
STRAND 237 239 {ECO:0000244|PDB:966C}.
HELIX 250 260 {ECO:0000244|PDB:1HFC}.
STRAND 285 290 {ECO:0000244|PDB:1SU3}.
STRAND 293 298 {ECO:0000244|PDB:1SU3}.
STRAND 301 304 {ECO:0000244|PDB:1SU3}.
STRAND 309 311 {ECO:0000244|PDB:1SU3}.
STRAND 313 316 {ECO:0000244|PDB:1SU3}.
HELIX 317 319 {ECO:0000244|PDB:1SU3}.
STRAND 330 334 {ECO:0000244|PDB:1SU3}.
HELIX 335 337 {ECO:0000244|PDB:1SU3}.
STRAND 339 344 {ECO:0000244|PDB:1SU3}.
STRAND 347 352 {ECO:0000244|PDB:1SU3}.
STRAND 361 363 {ECO:0000244|PDB:1SU3}.
HELIX 364 368 {ECO:0000244|PDB:1SU3}.
STRAND 379 382 {ECO:0000244|PDB:1SU3}.
TURN 384 386 {ECO:0000244|PDB:1SU3}.
STRAND 388 393 {ECO:0000244|PDB:1SU3}.
STRAND 396 401 {ECO:0000244|PDB:1SU3}.
TURN 402 405 {ECO:0000244|PDB:1SU3}.
STRAND 412 414 {ECO:0000244|PDB:1SU3}.
HELIX 415 418 {ECO:0000244|PDB:1SU3}.
STRAND 427 432 {ECO:0000244|PDB:1SU3}.
STRAND 435 440 {ECO:0000244|PDB:1SU3}.
STRAND 443 448 {ECO:0000244|PDB:1SU3}.
TURN 449 452 {ECO:0000244|PDB:1SU3}.
STRAND 453 459 {ECO:0000244|PDB:1SU3}.
TURN 460 463 {ECO:0000244|PDB:1SU3}.
SEQUENCE 469 AA; 54007 MW; 4B1361DCF4C54B20 CRC64;
MHSFPPLLLL LFWGVVSHSF PATLETQEQD VDLVQKYLEK YYNLKNDGRQ VEKRRNSGPV
VEKLKQMQEF FGLKVTGKPD AETLKVMKQP RCGVPDVAQF VLTEGNPRWE QTHLTYRIEN
YTPDLPRADV DHAIEKAFQL WSNVTPLTFT KVSEGQADIM ISFVRGDHRD NSPFDGPGGN
LAHAFQPGPG IGGDAHFDED ERWTNNFREY NLHRVAAHEL GHSLGLSHST DIGALMYPSY
TFSGDVQLAQ DDIDGIQAIY GRSQNPVQPI GPQTPKACDS KLTFDAITTI RGEVMFFKDR
FYMRTNPFYP EVELNFISVF WPQLPNGLEA AYEFADRDEV RFFKGNKYWA VQGQNVLHGY
PKDIYSSFGF PRTVKHIDAA LSEENTGKTY FFVANKYWRY DEYKRSMDPG YPKMIAHDFP
GIGHKVDAVF MKDGFFYFFH GTRQYKFDPK TKRILTLQKA NSWFNCRKN


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