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Collagenase 3 (EC 3.4.24.-) (Matrix metalloproteinase-13) (MMP-13)

 MMP13_HUMAN             Reviewed;         471 AA.
P45452; A8K846; B2RCZ3; Q6NWN6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-OCT-2017, entry version 185.
RecName: Full=Collagenase 3;
EC=3.4.24.-;
AltName: Full=Matrix metalloproteinase-13;
Short=MMP-13;
Flags: Precursor;
Name=MMP13;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Mammary carcinoma;
PubMed=8207000;
Freije J.M.P., Diez-Itza I., Balbin M., Sanchez L.M., Blasco R.,
Tolivia J., Lopez-Otin C.;
"Molecular cloning and expression of collagenase-3, a novel human
matrix metalloproteinase produced by breast carcinomas.";
J. Biol. Chem. 269:16766-16773(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=9562863;
Willmroth F., Peter H.H., Conca W.;
"A matrix metalloproteinase gene expressed in human T lymphocytes is
identical with collagenase 3 from breast carcinomas.";
Immunobiology 198:375-384(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Esophagus, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-390.
NIEHS SNPs program;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
PROTEIN SEQUENCE OF 20-27 AND 104-118, PROPEPTIDE, AUTOCATALYTIC
PROCESSING, CATALYTIC ACTIVITY, FUNCTION, GLYCOSYLATION AT ASN-117,
SUBCELLULAR LOCATION, ENZYME REGULATION, AND INTERACTION WITH TIMP1;
TIMP2 AND TIMP3.
PubMed=8576151; DOI=10.1074/jbc.271.3.1544;
Knaeuper V., Lopez-Otin C., Smith B., Knight G., Murphy G.;
"Biochemical characterization of human collagenase-3.";
J. Biol. Chem. 271:1544-1550(1996).
[7]
PARTIAL PROTEIN SEQUENCE, PROPEPTIDE, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=8663255; DOI=10.1074/jbc.271.29.17124;
Knaeuper V., Will H., Lopez-Otin C., Smith B., Atkinson S.J.,
Stanton H., Hembry R.M., Murphy G.;
"Cellular mechanisms for human procollagenase-3 (MMP-13) activation.
Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to
generate active enzyme.";
J. Biol. Chem. 271:17124-17131(1996).
[8]
FUNCTION.
PubMed=8603731; DOI=10.1016/0014-5793(95)01539-6;
Fosang A.J., Last K., Knaeuper V., Murphy G., Neame P.J.;
"Degradation of cartilage aggrecan by collagenase-3 (MMP-13).";
FEBS Lett. 380:17-20(1996).
[9]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=8798568; DOI=10.1074/jbc.271.38.23577;
Borden P., Solymar D., Sucharczuk A., Lindman B., Cannon P.,
Heller R.A.;
"Cytokine control of interstitial collagenase and collagenase-3 gene
expression in human chondrocytes.";
J. Biol. Chem. 271:23577-23581(1996).
[10]
TISSUE SPECIFICITY, AND INDUCTION BY TGFB1.
PubMed=9056642;
DOI=10.1002/(SICI)1097-0177(199703)208:3<387::AID-AJA9>3.0.CO;2-E;
Johansson N., Saarialho-Kere U., Airola K., Herva R., Nissinen L.,
Westermarck J., Vuorio E., Heino J., Kaehaeri V.M.;
"Collagenase-3 (MMP-13) is expressed by hypertrophic chondrocytes,
periosteal cells, and osteoblasts during human fetal bone
development.";
Dev. Dyn. 208:387-397(1997).
[11]
DOMAIN, CATALYTIC ACTIVITY, AUTOCATALYTIC PROCESSING, FUNCTION,
INTERACTION WITH TIMP1; TIMP2 AND TIMP3, AND ENZYME REGULATION.
PubMed=9065415; DOI=10.1074/jbc.272.12.7608;
Knaeuper V., Cowell S., Smith B., Lopez-Otin C., O'Shea M., Morris H.,
Zardi L., Murphy G.;
"The role of the C-terminal domain of human collagenase-3 (MMP-13) in
the activation of procollagenase-3, substrate specificity, and tissue
inhibitor of metalloproteinase interaction.";
J. Biol. Chem. 272:7608-7616(1997).
[12]
INVOLVEMENT IN MDST, AND VARIANT MDST GLY-207.
PubMed=24648384; DOI=10.1002/ajmg.a.36431;
Bonafe L., Liang J., Gorna M.W., Zhang Q., Ha-Vinh R.,
Campos-Xavier A.B., Unger S., Beckmann J.S., Le Bechec A.,
Stevenson B., Giedion A., Liu X., Superti-Furga G., Wang W., Spahr A.,
Superti-Furga A.;
"MMP13 mutations are the cause of recessive metaphyseal dysplasia,
Spahr type.";
Am. J. Med. Genet. A 164A:1175-1179(2014).
[13]
PHOSPHORYLATION AT TYR-366.
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).
[14]
INVOLVEMENT IN MDST.
PubMed=24781753; DOI=10.1038/ejhg.2014.76;
Li D., Weber D.R., Deardorff M.A., Hakonarson H., Levine M.A.;
"Exome sequencing reveals a nonsense mutation in MMP13 as a new cause
of autosomal recessive metaphyseal anadysplasia.";
Eur. J. Hum. Genet. 23:264-266(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 265-471 IN COMPLEX WITH
CALCIUM, AND DISULFIDE BOND.
PubMed=8969305; DOI=10.1006/jmbi.1996.0661;
Gomis-Rueth F.-X., Gohlke U., Betz M., Knaeuper V., Murphy G.,
Lopez-Otin C., Bode W.;
"The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure
of its C-terminal haemopexin-like domain.";
J. Mol. Biol. 264:556-566(1996).
[16]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 104-271 IN COMPLEXES WITH
SYNTHETIC INHIBITORS; CALCIUM AND ZINC, PROPEPTIDE, AND AUTOCATALYTIC
PROCESSING.
PubMed=10074939; DOI=10.1038/6657;
Lovejoy B., Welch A.R., Carr S., Luong C., Broka C., Hendricks R.T.,
Campbell J.A., Walker K.A., Martin R., Van Wart H., Browner M.F.;
"Crystal structures of MMP-1 and -13 reveal the structural basis for
selectivity of collagenase inhibitors.";
Nat. Struct. Biol. 6:217-221(1999).
[17]
STRUCTURE BY NMR OF 104-274 IN COMPLEX WITH CALCIUM AND ZINC.
PubMed=10926524; DOI=10.1006/jmbi.2000.3988;
Zhang X., Gonnella N.C., Koehn J., Pathak N., Ganu V., Melton R.,
Parker D., Hu S.I., Nam K.Y.;
"Solution structure of the catalytic domain of human collagenase-3
(MMP-13) complexed to a potent non-peptidic sulfonamide inhibitor:
binding comparison with stromelysin-1 and collagenase-1.";
J. Mol. Biol. 301:513-524(2000).
[18]
STRUCTURE BY NMR OF 104-268 IN COMPLEX WITH CALCIUM AND ZINC, AND
CATALYTIC ACTIVITY.
PubMed=10986126; DOI=10.1006/jmbi.2000.4082;
Moy F.J., Chanda P.K., Chen J.M., Cosmi S., Edris W., Levin J.I.,
Powers R.;
"High-resolution solution structure of the catalytic fragment of human
collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor.";
J. Mol. Biol. 302:671-689(2000).
[19]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 104-271 IN COMPLEX WITH
CALCIUM AND ZINC, COFACTOR, AND CATALYTIC ACTIVITY.
PubMed=15780611; DOI=10.1016/j.bmcl.2005.02.038;
Blagg J.A., Noe M.C., Wolf-Gouveia L.A., Reiter L.A., Laird E.R.,
Chang S.P., Danley D.E., Downs J.T., Elliott N.C., Eskra J.D.,
Griffiths R.J., Hardink J.R., Haugeto A.I., Jones C.S., Liras J.L.,
Lopresti-Morrow L.L., Mitchell P.G., Pandit J., Robinson R.P.,
Subramanyam C., Vaughn-Bowser M.L., Yocum S.A.;
"Potent pyrimidinetrione-based inhibitors of MMP-13 with enhanced
selectivity over MMP-14.";
Bioorg. Med. Chem. Lett. 15:1807-1810(2005).
[20]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 104-274 IN COMPLEX WITH
CALCIUM AND ZINC, COFACTOR, AND CATALYTIC ACTIVITY.
PubMed=15734645; DOI=10.1016/j.chembiol.2004.11.014;
Engel C.K., Pirard B., Schimanski S., Kirsch R., Habermann J.,
Klingler O., Schlotte V., Weithmann K.U., Wendt K.U.;
"Structural basis for the highly selective inhibition of MMP-13.";
Chem. Biol. 12:181-189(2005).
[21]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 104-270 IN COMPLEX WITH
CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION IN
CARTILAGE DEGRADATION.
PubMed=17623656; DOI=10.1074/jbc.M703286200;
Johnson A.R., Pavlovsky A.G., Ortwine D.F., Prior F., Man C.F.,
Bornemeier D.A., Banotai C.A., Mueller W.T., McConnell P., Yan C.,
Baragi V., Lesch C., Roark W.H., Wilson M., Datta K., Guzman R.,
Han H.K., Dyer R.D.;
"Discovery and characterization of a novel inhibitor of matrix
metalloprotease-13 that reduces cartilage damage in vivo without joint
fibroplasia side effects.";
J. Biol. Chem. 282:27781-27791(2007).
[22]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 104-268 IN COMPLEX WITH
TIMP2; CALCIUM AND ZINC, AND INTERACTION WITH TIMP2.
PubMed=17196980; DOI=10.1016/j.jmb.2006.11.072;
Maskos K., Lang R., Tschesche H., Bode W.;
"Flexibility and variability of TIMP binding: X-ray structure of the
complex between collagenase-3/MMP-13 and TIMP-2.";
J. Mol. Biol. 366:1222-1231(2007).
[23]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-274 IN COMPLEX WITH
CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, AND FUNCTION.
PubMed=19422229; DOI=10.1021/jm801394m;
Monovich L.G., Tommasi R.A., Fujimoto R.A., Blancuzzi V., Clark K.,
Cornell W.D., Doti R., Doughty J., Fang J., Farley D., Fitt J.,
Ganu V., Goldberg R., Goldstein R., Lavoie S., Kulathila R.,
Macchia W., Parker D.T., Melton R., O'Byrne E., Pastor G., Pellas T.,
Quadros E., Reel N., Roland D.M., Sakane Y., Singh H., Skiles J.,
Somers J., Toscano K., Wigg A., Zhou S., Zhu L., Shieh W.C., Xue S.,
McQuire L.W.;
"Discovery of potent, selective, and orally active carboxylic acid
based inhibitors of matrix metalloproteinase-13.";
J. Med. Chem. 52:3523-3538(2009).
[24]
X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 104-270 IN COMPLEX WITH
CALCIUM AND ZINC, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=20005097; DOI=10.1016/j.bmcl.2009.11.081;
Schnute M.E., O'Brien P.M., Nahra J., Morris M., Howard Roark W.,
Hanau C.E., Ruminski P.G., Scholten J.A., Fletcher T.R., Hamper B.C.,
Carroll J.N., Patt W.C., Shieh H.S., Collins B., Pavlovsky A.G.,
Palmquist K.E., Aston K.W., Hitchcock J., Rogers M.D., McDonald J.,
Johnson A.R., Munie G.E., Wittwer A.J., Man C.F., Settle S.L.,
Nemirovskiy O., Vickery L.E., Agawal A., Dyer R.D., Sunyer T.;
"Discovery of (pyridin-4-yl)-2H-tetrazole as a novel scaffold to
identify highly selective matrix metalloproteinase-13 inhibitors for
the treatment of osteoarthritis.";
Bioorg. Med. Chem. Lett. 20:576-580(2010).
[25]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 104-267 IN COMPLEX WITH
CALCIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, AND FUNCTION.
PubMed=20726512; DOI=10.1021/jm100669j;
Becker D.P., Barta T.E., Bedell L.J., Boehm T.L., Bond B.R.,
Carroll J., Carron C.P., Decrescenzo G.A., Easton A.M., Freskos J.N.,
Funckes-Shippy C.L., Heron M., Hockerman S., Howard C.P., Kiefer J.R.,
Li M.H., Mathis K.J., McDonald J.J., Mehta P.P., Munie G.E.,
Sunyer T., Swearingen C.A., Villamil C.I., Welsch D., Williams J.M.,
Yu Y., Yao J.;
"Orally active MMP-1 sparing alpha-tetrahydropyranyl and alpha-
piperidinyl sulfone matrix metalloproteinase (MMP) inhibitors with
efficacy in cancer, arthritis, and cardiovascular disease.";
J. Med. Chem. 53:6653-6680(2010).
[26]
X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 104-272 IN COMPLEX WITH
CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
FUNCTION.
PubMed=22689580; DOI=10.1074/jbc.M112.380782;
Devel L., Beau F., Amoura M., Vera L., Cassar-Lajeunesse E.,
Garcia S., Czarny B., Stura E.A., Dive V.;
"Simple pseudo-dipeptides with a P2' glutamate: a novel inhibitor
family of matrix metalloproteases and other metzincins.";
J. Biol. Chem. 287:26647-26656(2012).
[27]
X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 103-274 IN COMPLEX WITH
CALCIUM AND ZINC, COFACTOR, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=23810497; DOI=10.1016/j.bmcl.2013.05.089;
De Savi C., Waterson D., Pape A., Lamont S., Hadley E., Mills M.,
Page K.M., Bowyer J., Maciewicz R.A.;
"Hydantoin based inhibitors of MMP13--discovery of AZD6605.";
Bioorg. Med. Chem. Lett. 23:4705-4712(2013).
[28]
X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 104-471 OF MUTANT ALA-223 IN
COMPLEX WITH CALCIUM AND ZINC, COFACTOR, DISULFIDE BOND, MUTAGENESIS
OF GLU-223, ACTIVE SITE, AND SUBUNIT.
PubMed=23913860; DOI=10.1096/fj.13-233601;
Stura E.A., Visse R., Cuniasse P., Dive V., Nagase H.;
"Crystal structure of full-length human collagenase 3 (MMP-13) with
peptides in the active site defines exosites in the catalytic
domain.";
FASEB J. 27:4395-4405(2013).
[29]
VARIANT SEMD-MO SER-75, CHARACTERIZATION OF VARIANT SEMD-MO SER-75,
AND FUNCTION IN BONE DEVELOPMENT.
PubMed=16167086; DOI=10.1172/JCI22900;
Kennedy A.M., Inada M., Krane S.M., Christie P.T., Harding B.,
Lopez-Otin C., Sanchez L.M., Pannett A.A.J., Dearlove A., Hartley C.,
Byrne M.H., Reed A.A.C., Nesbit M.A., Whyte M.P., Thakker R.V.;
"MMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type
(SEMD(MO).";
J. Clin. Invest. 115:2832-2842(2005).
[30]
VARIANTS MANDP1 SER-74; THR-91 AND ASN-232, AND FUNCTION IN BONE
DEVELOPMENT.
PubMed=19615667; DOI=10.1016/j.ajhg.2009.06.014;
Lausch E., Keppler R., Hilbert K., Cormier-Daire V., Nikkel S.,
Nishimura G., Unger S., Spranger J., Superti-Furga A., Zabel B.;
"Mutations in MMP9 and MMP13 determine the mode of inheritance and the
clinical spectrum of metaphyseal anadysplasia.";
Am. J. Hum. Genet. 85:168-178(2009).
-!- FUNCTION: Plays a role in the degradation of extracellular matrix
proteins including fibrillar collagen, fibronectin, TNC and ACAN.
Cleaves triple helical collagens, including type I, type II and
type III collagen, but has the highest activity with soluble type
II collagen. Can also degrade collagen type IV, type XIV and type
X. May also function by activating or degrading key regulatory
proteins, such as TGFB1 and CTGF. Plays a role in wound healing,
tissue remodeling, cartilage degradation, bone development, bone
mineralization and ossification. Required for normal embryonic
bone development and ossification. Plays a role in the healing of
bone fractures via endochondral ossification. Plays a role in
wound healing, probably by a mechanism that involves proteolytic
activation of TGFB1 and degradation of CTGF. Plays a role in
keratinocyte migration during wound healing. May play a role in
cell migration and in tumor cell invasion.
{ECO:0000269|PubMed:16167086, ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:19615667,
ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:8207000,
ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:8603731,
ECO:0000269|PubMed:8663255, ECO:0000269|PubMed:9065415}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:10074939,
ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305};
Note=Can bind about 5 Ca(2+) ions per subunit.
{ECO:0000269|PubMed:10074939, ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:10074939,
ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860};
Note=Binds 2 Zn(2+) ions per subunit.
{ECO:0000269|PubMed:10074939, ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860};
-!- ENZYME REGULATION: Inhibited by TIMP1, TIMP2 and TIMP3. Inhibited
by acetohydroxamic acid and other zinc chelators.
{ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:8576151,
ECO:0000269|PubMed:9065415}.
-!- SUBUNIT: Monomer. Interacts with TIMP1, TIMP2 and TIMP3. Binds
(via the C-terminal region) to collagen.
{ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8576151, ECO:0000269|PubMed:8969305,
ECO:0000269|PubMed:9065415}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305|PubMed:8576151}. Secreted
{ECO:0000269|PubMed:8576151}.
-!- TISSUE SPECIFICITY: Detected in fetal cartilage and calvaria, in
chondrocytes of hypertrophic cartilage in vertebrae and in the
dorsal end of ribs undergoing ossification, as well as in
osteoblasts and periosteal cells below the inner periosteal region
of ossified ribs. Detected in chondrocytes from in joint cartilage
that have been treated with TNF and IL1B, but not in untreated
chondrocytes. Detected in T lymphocytes. Detected in breast
carcinoma tissue. {ECO:0000269|PubMed:8207000,
ECO:0000269|PubMed:8798568, ECO:0000269|PubMed:9056642,
ECO:0000269|PubMed:9562863}.
-!- INDUCTION: Up-regulated by TNF and IL1B.
{ECO:0000269|PubMed:8798568, ECO:0000269|PubMed:9056642}.
-!- 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 (By similarity).
{ECO:0000250}.
-!- DOMAIN: The C-terminal region binds to collagen.
{ECO:0000269|PubMed:9065415}.
-!- PTM: The proenzyme is activated by removal of the propeptide; this
cleavage can be effected by other matrix metalloproteinases, such
as MMP2, MMP3 and MMP14 and may involve several cleavage steps.
Cleavage can also be autocatalytic, after partial maturation by
another protease or after treatment with 4-aminophenylmercuric
acetate (APMA) (in vitro).
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:8576151}.
-!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
{ECO:0000269|PubMed:25171405}.
-!- DISEASE: Spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO)
[MIM:602111]: A bone disease characterized by moderate to severe
metaphyseal changes, mild epiphyseal involvement, rhizomelic
shortening of the lower limbs with bowing of the femora and/or
tibiae, coxa vara, genu varum and pear-shaped vertebrae in
childhood. Epimetaphyseal changes improve with age.
{ECO:0000269|PubMed:16167086}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Metaphyseal anadysplasia 1 (MANDP1) [MIM:602111]: A bone
development disorder characterized by skeletal anomalies that
resolve spontaneously with age. Clinical characteristics are
evident from the first months of life and include slight shortness
of stature and a mild varus deformity of the legs. Patients attain
a normal stature in adolescence and show improvement or complete
resolution of varus deformity of the legs and rhizomelic
micromelia. {ECO:0000269|PubMed:19615667}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Metaphyseal dysplasia, Spahr type (MDST) [MIM:250400]: An
autosomal recessive, rare disease characterized by moderate short
stature, mild genua vara, and radiographic signs of metaphyseal
dysplasia, but no biochemical signs of rickets.
{ECO:0000269|PubMed:24648384, ECO:0000269|PubMed:24781753}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp13/";
-----------------------------------------------------------------------
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EMBL; X75308; CAA53056.1; -; mRNA.
EMBL; X81334; CAA57108.1; -; mRNA.
EMBL; AK292211; BAF84900.1; -; mRNA.
EMBL; AK315341; BAG37740.1; -; mRNA.
EMBL; AY741163; AAU13907.1; -; Genomic_DNA.
EMBL; BC067522; AAH67522.1; -; mRNA.
EMBL; BC067523; AAH67523.1; -; mRNA.
EMBL; BC074807; AAH74807.1; -; mRNA.
EMBL; BC074808; AAH74808.1; -; mRNA.
CCDS; CCDS8324.1; -.
PIR; A53711; A53711.
RefSeq; NP_002418.1; NM_002427.3.
UniGene; Hs.2936; -.
PDB; 1EUB; NMR; -; A=104-274.
PDB; 1FLS; NMR; -; A=104-268.
PDB; 1FM1; NMR; -; A=104-268.
PDB; 1PEX; X-ray; 2.70 A; A=265-471.
PDB; 1UC1; Model; -; A=1-471.
PDB; 1XUC; X-ray; 1.70 A; A/B=104-274.
PDB; 1XUD; X-ray; 1.80 A; A/B=104-274.
PDB; 1XUR; X-ray; 1.85 A; A/B=104-274.
PDB; 1YOU; X-ray; 2.30 A; A/B=104-271.
PDB; 1ZTQ; X-ray; 2.00 A; A/B/C/D=104-268.
PDB; 2D1N; X-ray; 2.37 A; A/B=104-269.
PDB; 2E2D; X-ray; 2.00 A; A=104-268.
PDB; 2OW9; X-ray; 1.74 A; A/B=104-270.
PDB; 2OZR; X-ray; 2.30 A; A/B/C/D/E/F/G/H=104-270.
PDB; 2PJT; X-ray; 2.80 A; A/B/C/D=104-268.
PDB; 2YIG; X-ray; 1.70 A; A/B=104-274.
PDB; 3ELM; X-ray; 1.90 A; A/B=104-274.
PDB; 3I7G; X-ray; 1.95 A; A/B=104-274.
PDB; 3I7I; X-ray; 2.21 A; A/B=104-274.
PDB; 3KEC; X-ray; 2.05 A; A/B=105-267.
PDB; 3KEJ; X-ray; 2.30 A; A/B=104-270.
PDB; 3KEK; X-ray; 1.97 A; A/B=104-270.
PDB; 3KRY; X-ray; 1.90 A; A/B/C/D=104-267.
PDB; 3LJZ; X-ray; 2.00 A; A/B/C/D=104-267.
PDB; 3O2X; X-ray; 1.90 A; A/B/C/D=105-267.
PDB; 3TVC; X-ray; 2.43 A; A=104-272.
PDB; 3WV1; X-ray; 1.98 A; A/B=104-274.
PDB; 3WV2; X-ray; 2.30 A; A/B=104-274.
PDB; 3WV3; X-ray; 1.60 A; A/B=104-274.
PDB; 3ZXH; X-ray; 1.30 A; A/B=104-274.
PDB; 456C; X-ray; 2.40 A; A/B=104-271.
PDB; 4A7B; X-ray; 2.20 A; A/B=104-272.
PDB; 4FU4; X-ray; 2.85 A; A/B=104-471, C/D=25-50.
PDB; 4FVL; X-ray; 2.44 A; A/B=104-471, C/D=31-50.
PDB; 4G0D; X-ray; 2.54 A; A/B/C/D=104-471, W/X/Y/Z=25-50.
PDB; 4JP4; X-ray; 1.43 A; A/B=103-274.
PDB; 4JPA; X-ray; 2.00 A; A/B=103-274.
PDB; 4L19; X-ray; 1.66 A; A/B=104-274.
PDB; 5B5O; X-ray; 1.20 A; A/B=103-274.
PDB; 5B5P; X-ray; 1.60 A; A/B=103-274.
PDB; 5BOT; X-ray; 1.85 A; A/B=104-274.
PDB; 5BOY; X-ray; 2.03 A; A/B=104-274.
PDB; 5BPA; X-ray; 1.79 A; A/B=104-274.
PDB; 5UWK; X-ray; 1.60 A; A/B=104-274.
PDB; 5UWL; X-ray; 2.55 A; A/B=104-274.
PDB; 5UWM; X-ray; 1.62 A; A/B=104-274.
PDB; 5UWN; X-ray; 3.20 A; A/B/C/D/E=104-274.
PDB; 830C; X-ray; 1.60 A; A/B=104-271.
PDBsum; 1EUB; -.
PDBsum; 1FLS; -.
PDBsum; 1FM1; -.
PDBsum; 1PEX; -.
PDBsum; 1UC1; -.
PDBsum; 1XUC; -.
PDBsum; 1XUD; -.
PDBsum; 1XUR; -.
PDBsum; 1YOU; -.
PDBsum; 1ZTQ; -.
PDBsum; 2D1N; -.
PDBsum; 2E2D; -.
PDBsum; 2OW9; -.
PDBsum; 2OZR; -.
PDBsum; 2PJT; -.
PDBsum; 2YIG; -.
PDBsum; 3ELM; -.
PDBsum; 3I7G; -.
PDBsum; 3I7I; -.
PDBsum; 3KEC; -.
PDBsum; 3KEJ; -.
PDBsum; 3KEK; -.
PDBsum; 3KRY; -.
PDBsum; 3LJZ; -.
PDBsum; 3O2X; -.
PDBsum; 3TVC; -.
PDBsum; 3WV1; -.
PDBsum; 3WV2; -.
PDBsum; 3WV3; -.
PDBsum; 3ZXH; -.
PDBsum; 456C; -.
PDBsum; 4A7B; -.
PDBsum; 4FU4; -.
PDBsum; 4FVL; -.
PDBsum; 4G0D; -.
PDBsum; 4JP4; -.
PDBsum; 4JPA; -.
PDBsum; 4L19; -.
PDBsum; 5B5O; -.
PDBsum; 5B5P; -.
PDBsum; 5BOT; -.
PDBsum; 5BOY; -.
PDBsum; 5BPA; -.
PDBsum; 5UWK; -.
PDBsum; 5UWL; -.
PDBsum; 5UWM; -.
PDBsum; 5UWN; -.
PDBsum; 830C; -.
ProteinModelPortal; P45452; -.
SMR; P45452; -.
BioGrid; 110465; 15.
STRING; 9606.ENSP00000260302; -.
BindingDB; P45452; -.
ChEMBL; CHEMBL280; -.
DrugBank; DB03033; 1-Methyloxy-4-Sulfone-Benzene.
DrugBank; DB02049; 2-{4-[4-(4-Chloro-Phenoxy)-Benzenesulfonyl]-Tetrahydro-Pyran-4-Yl}-N-Hydroxy-Acetamide.
DrugBank; DB01996; 3-Methylpyridine.
DrugBank; DB08490; 4-[4-(4-CHLORO-PHENOXY)-BENZENESULFONYLMETHYL]-TETRAHYDRO-PYRAN-4-CARBOXYLIC ACID HYDROXYAMIDE.
DrugBank; DB02697; Hydroxyaminovaline.
DrugBank; DB00786; Marimastat.
DrugBank; DB07013; TERT-BUTYL 4-({[4-(BUT-2-YN-1-YLAMINO)PHENYL]SULFONYL}METHYL)-4-[(HYDROXYAMINO)CARBONYL]PIPERIDINE-1-CARBOXYLATE.
DrugBank; DB02071; WAY-151693.
GuidetoPHARMACOLOGY; 1637; -.
MEROPS; M10.013; -.
iPTMnet; P45452; -.
PhosphoSitePlus; P45452; -.
BioMuta; MMP13; -.
DMDM; 1168998; -.
EPD; P45452; -.
PaxDb; P45452; -.
PeptideAtlas; P45452; -.
PRIDE; P45452; -.
DNASU; 4322; -.
Ensembl; ENST00000260302; ENSP00000260302; ENSG00000137745.
GeneID; 4322; -.
KEGG; hsa:4322; -.
UCSC; uc001phl.4; human.
CTD; 4322; -.
DisGeNET; 4322; -.
EuPathDB; HostDB:ENSG00000137745.11; -.
GeneCards; MMP13; -.
HGNC; HGNC:7159; MMP13.
MalaCards; MMP13; -.
MIM; 250400; phenotype.
MIM; 600108; gene.
MIM; 602111; phenotype.
neXtProt; NX_P45452; -.
OpenTargets; ENSG00000137745; -.
Orphanet; 1040; Metaphyseal anadysplasia.
Orphanet; 2501; Metaphyseal chondrodysplasia, Spahr type.
Orphanet; 93356; Spondyloepimetaphyseal dysplasia, Missouri type.
PharmGKB; PA30871; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P45452; -.
KO; K07994; -.
PhylomeDB; P45452; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.17; 2681.
BRENDA; 3.4.24.35; 2681.
BRENDA; 3.4.24.65; 2681.
BRENDA; 3.4.24.B4; 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-2022090; Assembly of collagen fibrils and other multimeric structures.
SIGNOR; P45452; -.
EvolutionaryTrace; P45452; -.
GeneWiki; Matrix_metallopeptidase_13; -.
GenomeRNAi; 4322; -.
PMAP-CutDB; P45452; -.
PRO; PR:P45452; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137745; -.
CleanEx; HS_MMP13; -.
ExpressionAtlas; P45452; baseline and differential.
Genevisible; P45452; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0060349; P:bone morphogenesis; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; IDA:UniProtKB.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0003417; P:growth plate cartilage development; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR028711; Collagenase_3.
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.
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.
PANTHER; PTHR10201:SF165; PTHR10201:SF165; 1.
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; Calcium; Collagen degradation; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism;
Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 19 {ECO:0000269|PubMed:8576151}.
PROPEP 20 103 Activation peptide.
{ECO:0000269|PubMed:8576151}.
/FTId=PRO_0000028788.
CHAIN 104 471 Collagenase 3.
/FTId=PRO_0000028789.
REPEAT 281 330 Hemopexin 1.
REPEAT 331 377 Hemopexin 2.
REPEAT 379 427 Hemopexin 3.
REPEAT 428 471 Hemopexin 4.
REGION 176 246 Interaction with TIMP2.
REGION 268 471 Interaction with collagen.
MOTIF 94 101 Cysteine switch. {ECO:0000250}.
ACT_SITE 223 223 {ECO:0000305|PubMed:23913860}.
METAL 96 96 Zinc 2; in inhibited form. {ECO:0000250}.
METAL 128 128 Calcium 1. {ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 162 162 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 172 172 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 174 174 Zinc 1. {ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 179 179 Calcium 3. {ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 180 180 Calcium 3; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 182 182 Calcium 3; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 184 184 Calcium 3; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 187 187 Zinc 1; via tele nitrogen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 194 194 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 196 196 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 198 198 Calcium 2. {ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 200 200 Zinc 1; via pros nitrogen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 202 202 Calcium 3. {ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 203 203 Calcium 1. {ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 205 205 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 205 205 Calcium 3. {ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 222 222 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 226 226 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 232 232 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 240 240 Zinc 2; via carbonyl oxygen; catalytic.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860}.
METAL 291 291 Calcium 4; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 293 293 Calcium 5; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 335 335 Calcium 4; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 337 337 Calcium 5; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 383 383 Calcium 4; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 385 385 Calcium 5; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 432 432 Calcium 4; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
METAL 434 434 Calcium 5; via carbonyl oxygen.
{ECO:0000269|PubMed:10926524,
ECO:0000269|PubMed:10986126,
ECO:0000269|PubMed:15734645,
ECO:0000269|PubMed:15780611,
ECO:0000269|PubMed:17196980,
ECO:0000269|PubMed:17623656,
ECO:0000269|PubMed:19422229,
ECO:0000269|PubMed:20005097,
ECO:0000269|PubMed:20726512,
ECO:0000269|PubMed:22689580,
ECO:0000269|PubMed:23810497,
ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
MOD_RES 366 366 Phosphotyrosine; by PKDCC.
{ECO:0000303|PubMed:25171405}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8576151}.
CARBOHYD 152 152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 284 471 {ECO:0000269|PubMed:23913860,
ECO:0000269|PubMed:8969305}.
VARIANT 2 2 H -> L (in dbSNP:rs554797).
/FTId=VAR_011971.
VARIANT 74 74 F -> S (in MANDP1; dbSNP:rs121909498).
{ECO:0000269|PubMed:19615667}.
/FTId=VAR_063432.
VARIANT 75 75 F -> S (in SEMD-MO; abnormal
intracellular autoactivation and
autodegradation within the ER/Golgi
resulting in the secretion of small and
inactive fragments; dbSNP:rs121909497).
{ECO:0000269|PubMed:16167086}.
/FTId=VAR_032753.
VARIANT 91 91 M -> T (in MANDP1; dbSNP:rs121909499).
{ECO:0000269|PubMed:19615667}.
/FTId=VAR_063433.
VARIANT 207 207 W -> G (in MDST; dbSNP:rs140059558).
{ECO:0000269|PubMed:24648384}.
/FTId=VAR_073418.
VARIANT 232 232 H -> N (in MANDP1; dbSNP:rs121909500).
{ECO:0000269|PubMed:19615667}.
/FTId=VAR_063434.
VARIANT 390 390 D -> G (in dbSNP:rs17860568).
{ECO:0000269|Ref.4}.
/FTId=VAR_020534.
MUTAGEN 223 223 E->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:23913860}.
CONFLICT 147 147 D -> G (in Ref. 3; BAF84900).
{ECO:0000305}.
CONFLICT 278 278 P -> L (in Ref. 5; AAH67523).
{ECO:0000305}.
CONFLICT 438 438 N -> D (in Ref. 3; BAG37740).
{ECO:0000305}.
HELIX 33 36 {ECO:0000244|PDB:4FVL}.
HELIX 38 41 {ECO:0000244|PDB:4G0D}.
STRAND 44 48 {ECO:0000244|PDB:4FVL}.
STRAND 109 111 {ECO:0000244|PDB:3ZXH}.
STRAND 114 122 {ECO:0000244|PDB:5B5O}.
STRAND 127 129 {ECO:0000244|PDB:3I7I}.
HELIX 131 146 {ECO:0000244|PDB:5B5O}.
STRAND 148 150 {ECO:0000244|PDB:3O2X}.
STRAND 152 159 {ECO:0000244|PDB:5B5O}.
STRAND 162 168 {ECO:0000244|PDB:5B5O}.
STRAND 173 175 {ECO:0000244|PDB:5B5O}.
STRAND 180 183 {ECO:0000244|PDB:5B5O}.
STRAND 186 188 {ECO:0000244|PDB:5B5O}.
STRAND 191 193 {ECO:0000244|PDB:5B5O}.
TURN 194 197 {ECO:0000244|PDB:5B5O}.
STRAND 199 202 {ECO:0000244|PDB:5B5O}.
STRAND 207 215 {ECO:0000244|PDB:5B5O}.
HELIX 216 228 {ECO:0000244|PDB:5B5O}.
STRAND 235 237 {ECO:0000244|PDB:1EUB}.
STRAND 241 243 {ECO:0000244|PDB:5B5O}.
STRAND 249 251 {ECO:0000244|PDB:3KRY}.
HELIX 256 266 {ECO:0000244|PDB:5B5O}.
STRAND 269 271 {ECO:0000244|PDB:5B5O}.
STRAND 291 296 {ECO:0000244|PDB:4FVL}.
STRAND 299 304 {ECO:0000244|PDB:4FVL}.
STRAND 307 311 {ECO:0000244|PDB:4FVL}.
STRAND 313 316 {ECO:0000244|PDB:1PEX}.
STRAND 319 322 {ECO:0000244|PDB:4FVL}.
HELIX 323 326 {ECO:0000244|PDB:4FVL}.
STRAND 335 340 {ECO:0000244|PDB:4FVL}.
HELIX 341 343 {ECO:0000244|PDB:4FVL}.
STRAND 345 350 {ECO:0000244|PDB:4FVL}.
STRAND 353 358 {ECO:0000244|PDB:4FVL}.
STRAND 367 369 {ECO:0000244|PDB:4FVL}.
HELIX 370 373 {ECO:0000244|PDB:4FVL}.
STRAND 384 387 {ECO:0000244|PDB:4FVL}.
TURN 389 391 {ECO:0000244|PDB:4FVL}.
STRAND 393 398 {ECO:0000244|PDB:4FVL}.
STRAND 401 406 {ECO:0000244|PDB:4FVL}.
TURN 407 410 {ECO:0000244|PDB:4FVL}.
HELIX 420 423 {ECO:0000244|PDB:4FVL}.
STRAND 432 437 {ECO:0000244|PDB:4FVL}.
STRAND 440 445 {ECO:0000244|PDB:4FVL}.
STRAND 448 453 {ECO:0000244|PDB:4FVL}.
TURN 454 457 {ECO:0000244|PDB:4FVL}.
STRAND 458 464 {ECO:0000244|PDB:4FVL}.
HELIX 465 469 {ECO:0000244|PDB:4FVL}.
SEQUENCE 471 AA; 53820 MW; E110F50628B57B60 CRC64;
MHPGVLAAFL FLSWTHCRAL PLPSGGDEDD LSEEDLQFAE RYLRSYYHPT NLAGILKENA
ASSMTERLRE MQSFFGLEVT GKLDDNTLDV MKKPRCGVPD VGEYNVFPRT LKWSKMNLTY
RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP LNFTRLHDGI ADIMISFGIK EHGDFYPFDG
PSGLLAHAFP PGPNYGGDAH FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM
FPIYTYTGKS HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET
MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR GRKFWALNGY
DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN QVWRYDDTNH IMDKDYPRLI
EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF EYSIWSNRIV RVMPANSILW C


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