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Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9]

 MMP9_HUMAN              Reviewed;         707 AA.
P14780; B2R7V9; Q3LR70; Q8N725; Q9H4Z1; Q9UCJ9; Q9UCL1; Q9UDK2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 3.
27-SEP-2017, entry version 222.
RecName: Full=Matrix metalloproteinase-9;
Short=MMP-9;
EC=3.4.24.35;
AltName: Full=92 kDa gelatinase;
AltName: Full=92 kDa type IV collagenase;
AltName: Full=Gelatinase B;
Short=GELB;
Contains:
RecName: Full=67 kDa matrix metalloproteinase-9;
Contains:
RecName: Full=82 kDa matrix metalloproteinase-9;
Flags: Precursor;
Name=MMP9; Synonyms=CLG4B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-37, AND VARIANTS
ARG-279 AND PRO-574.
PubMed=2551898;
Wilhelm S.M., Collier I.E., Marmer B.L., Eisen A.Z., Grant G.A.,
Goldberg G.I.;
"SV40-transformed human lung fibroblasts secrete a 92-kDa type IV
collagenase which is identical to that secreted by normal human
macrophages.";
J. Biol. Chem. 264:17213-17221(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1653238;
Huhtala P., Tuuttila A., Chow L.T., Lohi J., Keski-Oja J.,
Tryggvason K.;
"Complete structure of the human gene for 92-kDa type IV collagenase.
Divergent regulation of expression for the 92- and 72-kilodalton
enzyme genes in HT-1080 cells.";
J. Biol. Chem. 266:16485-16490(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-574.
TISSUE=Umbilical cord blood;
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 VARIANTS VAL-20; LYS-127;
ARG-279; PRO-574 AND GLN-668.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-20; HIS-239;
VAL-571; PRO-574 AND GLN-668.
NIEHS SNPs program;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-279 AND
PRO-574.
TISSUE=B-cell;
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 1-11.
PubMed=8426746;
Sato H., Seiki M.;
"Regulatory mechanism of 92 kDa type IV collagenase gene expression
which is associated with invasiveness of tumor cells.";
Oncogene 8:395-405(1993).
[9]
PROTEIN SEQUENCE OF 20-39, AND GLYCOSYLATION.
TISSUE=Neutrophil;
PubMed=1464361;
Kjeldsen L., Bjerrum O.W., Hovgaard D., Johnsen A.H., Sehested M.,
Borregaard N.;
"Human neutrophil gelatinase: a marker for circulating blood
neutrophils. Purification and quantitation by enzyme linked
immunosorbent assay.";
Eur. J. Haematol. 49:180-191(1992).
[10]
PROTEIN SEQUENCE OF 20-37.
PubMed=1653055; DOI=10.1016/1043-4666(91)90021-5;
van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F.,
Auwerx J., van Damme J., Opdenakker G.;
"The cytokine-protease connection: identification of a 96-kD THP-1
gelatinase and regulation by interleukin-1 and cytokine inducers.";
Cytokine 3:231-239(1991).
[11]
PROTEIN SEQUENCE OF 20-34; 60-71 AND 107-118, INDUCTION, AND
PROTEOLYTIC PROCESSING BY MMP3.
PubMed=1371271;
Ogata Y., Enghild J.J., Nagase H.;
"Matrix metalloproteinase 3 (stromelysin) activates the precursor for
the human matrix metalloproteinase 9.";
J. Biol. Chem. 267:3581-3584(1992).
[12]
PROTEIN SEQUENCE OF 20-32 AND 94-111, PROTEOLYTIC PROCESSING, AND
INDUCTION.
TISSUE=Fibrosarcoma;
PubMed=1400481;
Okada Y., Gonoji Y., Naka K., Tomita K., Nakanishi I., Iwata K.,
Yamashita K., Hayakawa T.;
"Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase)
from HT 1080 human fibrosarcoma cells. Purification and activation of
the precursor and enzymic properties.";
J. Biol. Chem. 267:21712-21719(1992).
[13]
PROTEIN SEQUENCE OF 20-27; 60-67; 94-101 AND 107-113.
PubMed=7669817; DOI=10.1016/0167-4838(95)00086-A;
Sang Q.X., Birkedal-Hansen H., Van Wart H.E.;
"Proteolytic and non-proteolytic activation of human neutrophil
progelatinase B.";
Biochim. Biophys. Acta 1251:99-108(1995).
[14]
PROTEIN SEQUENCE OF 28-60.
TISSUE=Neutrophil;
PubMed=1645657; DOI=10.1111/j.1432-1033.1991.tb16027.x;
Masure S., Proost P., van Damme J., Opdenakker G.;
"Purification and identification of 91-kDa neutrophil gelatinase.
Release by the activating peptide interleukin-8.";
Eur. J. Biochem. 198:391-398(1991).
[15]
PROTEIN SEQUENCE OF 28-37.
PubMed=1932376;
Opdenakker G., Masure S., Grillet B., Van Damme J.;
"Cytokine-mediated regulation of human leukocyte gelatinases and role
in arthritis.";
Lymphokine Cytokine Res. 10:317-324(1991).
[16]
PROTEIN SEQUENCE OF 93-115, FUNCTION, AND CATALYTIC ACTIVITY.
TISSUE=Blood;
PubMed=1480034;
Tschesche H., Knaeuper V., Kraemer S., Michaelis J., Oberhoff R.,
Reinke H.;
"Latent collagenase and gelatinase from human neutrophils and their
activation.";
Matrix Suppl. 1:245-255(1992).
[17]
CHARACTERIZATION.
Kang K., Lee D.-H.;
"Purification and characterization of human 92-kDa type IV collagenase
(gelatinase B).";
Exp. Mol. Med. 28:161-165(1996).
[18]
SUBUNIT.
PubMed=10644727; DOI=10.1074/jbc.275.4.2661;
Olson M.W., Bernardo M.M., Pietila M., Gervasi D.C., Toth M.,
Kotra L.P., Massova I., Mobashery S., Fridman R.;
"Characterization of the monomeric and dimeric forms of latent and
active matrix metalloproteinase-9. Differential rates for activation
by stromelysin 1.";
J. Biol. Chem. 275:2661-2668(2000).
[19]
ENZYME REGULATION.
PubMed=11179305; DOI=10.1128/IAI.69.3.1402-1408.2001;
Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F.,
Oppenheim F.G.;
"Salivary histatin 5 is an inhibitor of both host and bacterial
enzymes implicated in periodontal disease.";
Infect. Immun. 69:1402-1408(2001).
[20]
PROTEOLYTIC PROCESSING OF KISS1.
PubMed=12879005; DOI=10.1038/sj.onc.1206542;
Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y.,
Seiki M., Sato H.;
"Cleavage of metastasis suppressor gene product KiSS-1
protein/metastin by matrix metalloproteinases.";
Oncogene 22:4617-4626(2003).
[21]
INTERACTION WITH ECM1, AND ENZYME REGULATION.
PubMed=16512877; DOI=10.1111/j.0906-6705.2006.00409.x;
Fujimoto N., Terlizzi J., Aho S., Brittingham R., Fertala A.,
Oyama N., McGrath J.A., Uitto J.;
"Extracellular matrix protein 1 inhibits the activity of matrix
metalloproteinase 9 through high-affinity protein/protein
interactions.";
Exp. Dermatol. 15:300-307(2006).
[22]
INVOLVEMENT IN SUSCEPTIBILITY TO IDD.
PubMed=18455130; DOI=10.1016/j.ajhg.2008.03.013;
Hirose Y., Chiba K., Karasugi T., Nakajima M., Kawaguchi Y.,
Mikami Y., Furuichi T., Mio F., Miyake A., Miyamoto T., Ozaki K.,
Takahashi A., Mizuta H., Kubo T., Kimura T., Tanaka T., Toyama Y.,
Ikegawa S.;
"A functional polymorphism in THBS2 that affects alternative splicing
and MMP binding is associated with lumbar-disc herniation.";
Am. J. Hum. Genet. 82:1122-1129(2008).
[23]
INVOLVEMENT IN MANDP2.
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).
[24]
INDUCTION.
PubMed=19893577; DOI=10.1038/embor.2009.233;
Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M.,
Ohwada S., Akiyama T.;
"The adenomatous polyposis coli-associated exchange factors Asef and
Asef2 are required for adenoma formation in Apc(Min/+)mice.";
EMBO Rep. 10:1355-1362(2009).
[25]
INDUCTION BY M.BOVIS MPB83.
TISSUE=Monocytic leukemia;
PubMed=20800577; DOI=10.1016/j.bbrc.2010.08.085;
Chambers M.A., Whelan A.O., Spallek R., Singh M., Coddeville B.,
Guerardel Y., Elass E.;
"Non-acylated Mycobacterium bovis glycoprotein MPB83 binds to TLR1/2
and stimulates production of matrix metalloproteinase 9.";
Biochem. Biophys. Res. Commun. 400:403-408(2010).
[26]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-444 IN COMPLEX WITH ZINC
AND MAGNESIUM IONS.
PubMed=12077439; DOI=10.1107/S0907444902007849;
Elkins P.A., Ho Y.S., Smith W.W., Janson C.A., D'Alessio K.J.,
McQueney M.S., Cummings M.D., Romanic A.M.;
"Structure of the C-terminally truncated human ProMMP9, a gelatin-
binding matrix metalloproteinase.";
Acta Crystallogr. D 58:1182-1192(2002).
[27]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 107-215 IN COMPLEX WITH
INHIBITOR; ZINC AND CALCIUM IONS, AND MUTAGENESIS OF GLU-402.
PubMed=12051944; DOI=10.1016/S0022-2836(02)00262-0;
Rowsell S., Hawtin P., Minshull C.A., Jepson H., Brockbank S.M.V.,
Barratt D.G., Slater A.M., McPheat W.L., Waterson D., Henney A.M.,
Pauptit R.A.;
"Crystal structure of human MMP9 in complex with a reverse hydroxamate
inhibitor.";
J. Mol. Biol. 319:173-181(2002).
[28]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 513-707, AND SUBUNIT.
PubMed=12126625; DOI=10.1016/S0022-2836(02)00558-2;
Cha H., Kopetzki E., Huber R., Lanzendoerfer M., Brandstetter H.;
"Structural basis of the adaptive molecular recognition by MMP9.";
J. Mol. Biol. 320:1065-1079(2002).
[29]
3D-STRUCTURE MODELING.
Mallena S.C., Sagajkar R.D.;
"Theoretical model of human type IV collagenase precursor.";
Submitted (APR-2002) to the PDB data bank.
[30]
VARIANTS VAL-20; LYS-82 AND ARG-279.
PubMed=10598806; DOI=10.1007/s004390051124;
Zhang B., Henney A., Eriksson P., Hamsten A., Watkins H., Ye S.;
"Genetic variation at the matrix metalloproteinase-9 locus on
chromosome 20q12.2-13.1.";
Hum. Genet. 105:418-423(1999).
-!- FUNCTION: May play an essential role in local proteolysis of the
extracellular matrix and in leukocyte migration. Could play a role
in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu
bond. Cleaves type IV and type V collagen into large C-terminal
three quarter fragments and shorter N-terminal one quarter
fragments. Degrades fibronectin but not laminin or Pz-peptide.
{ECO:0000269|PubMed:1480034}.
-!- CATALYTIC ACTIVITY: Cleavage of gelatin types I and V and collagen
types IV and V. {ECO:0000269|PubMed:1480034}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 3 Ca(2+) ions per subunit.;
-!- ENZYME REGULATION: Inhibited by histatin-3 1/24 (histatin-5).
Inhibited by ECM1. {ECO:0000269|PubMed:11179305,
ECO:0000269|PubMed:16512877}.
-!- SUBUNIT: Exists as monomer or homodimer; disulfide-linked. Exists
also as heterodimer with a 25 kDa protein. Macrophages and
transformed cell lines produce only the monomeric form. Interacts
with ECM1. {ECO:0000269|PubMed:10644727,
ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439,
ECO:0000269|PubMed:12126625, ECO:0000269|PubMed:16512877}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1382326, EBI-1382326;
Q16819:MEP1A; NbExp=2; IntAct=EBI-1382326, EBI-8153734;
Q16820:MEP1B; NbExp=2; IntAct=EBI-1382326, EBI-968418;
Q8IX30:SCUBE3; NbExp=2; IntAct=EBI-1382326, EBI-4479975;
P01033:TIMP1; NbExp=2; IntAct=EBI-1382326, EBI-712536;
P13611:VCAN; NbExp=3; IntAct=EBI-1382326, EBI-8515977;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000305}.
-!- TISSUE SPECIFICITY: Produced by normal alveolar macrophages and
granulocytes.
-!- INDUCTION: Activated by 4-aminophenylmercuric acetate and phorbol
ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK
signaling pathway in colorectal tumor cells.
{ECO:0000269|PubMed:1371271, ECO:0000269|PubMed:1400481,
ECO:0000269|PubMed:19893577}.
-!- INDUCTION: (Microbial infection) Expression induced by M.bovis
MPB83 (at protein level) (PubMed:20800577).
{ECO:0000269|PubMed:20800577}.
-!- 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.
-!- PTM: Processing of the precursor yields different active forms of
64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82
kDa matrix metalloproteinase-9. {ECO:0000269|PubMed:12879005,
ECO:0000269|PubMed:1371271, ECO:0000269|PubMed:1400481}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1464361}.
-!- DISEASE: Intervertebral disc disease (IDD) [MIM:603932]: A common
musculo-skeletal disorder caused by degeneration of intervertebral
disks of the lumbar spine. It results in low-back pain and
unilateral leg pain. {ECO:0000269|PubMed:18455130}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- DISEASE: Metaphyseal anadysplasia 2 (MANDP2) [MIM:613073]: 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.
-!- MISCELLANEOUS: In the arthritis patient this enzyme might
contribute to the pathogenesis of joint destruction and might
constitute a useful marker of disease status.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MMP9ID41408ch20q11.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp9/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/mmp9/";
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EMBL; J05070; AAA51539.1; -; mRNA.
EMBL; M68343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK313137; BAG35956.1; -; mRNA.
EMBL; AF538844; AAM97934.1; -; Genomic_DNA.
EMBL; DQ194553; ABA03169.1; -; Genomic_DNA.
EMBL; AL162458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006093; AAH06093.1; -; mRNA.
EMBL; D10051; BAA20967.1; -; Genomic_DNA.
CCDS; CCDS13390.1; -.
PIR; A34458; A34458.
RefSeq; NP_004985.2; NM_004994.2.
UniGene; Hs.297413; -.
PDB; 1GKC; X-ray; 2.30 A; A/B=107-443.
PDB; 1GKD; X-ray; 2.10 A; A/B=107-443.
PDB; 1ITV; X-ray; 1.95 A; A/B=513-707.
PDB; 1L6J; X-ray; 2.50 A; A=20-444.
PDB; 1LKG; Model; -; A=1-707.
PDB; 2OVX; X-ray; 2.00 A; A/B=110-443.
PDB; 2OVZ; X-ray; 2.00 A; A/B=110-443.
PDB; 2OW0; X-ray; 2.00 A; A/B=110-443.
PDB; 2OW1; X-ray; 2.20 A; A/B=110-443.
PDB; 2OW2; X-ray; 2.90 A; A/B=110-443.
PDB; 4H1Q; X-ray; 1.59 A; A/B=110-214, A/B=391-444.
PDB; 4H2E; X-ray; 2.90 A; A/B=107-461.
PDB; 4H3X; X-ray; 1.76 A; A/B=107-461.
PDB; 4H82; X-ray; 1.90 A; A/B/C/D=110-444.
PDB; 4HMA; X-ray; 1.94 A; A/B=110-214, A/B=391-444.
PDB; 4JIJ; X-ray; 1.70 A; A/B=107-444.
PDB; 4JQG; X-ray; 1.85 A; A/B=107-444.
PDB; 4WZV; X-ray; 1.65 A; A/B=110-444.
PDB; 4XCT; X-ray; 1.30 A; A=113-444.
PDB; 5CUH; X-ray; 1.83 A; A/B=107-444.
PDB; 5I12; X-ray; 1.59 A; A=113-444.
PDB; 5TH6; X-ray; 1.70 A; A/B/C/D=40-443.
PDB; 5TH9; X-ray; 3.00 A; A/B/C=40-443.
PDBsum; 1GKC; -.
PDBsum; 1GKD; -.
PDBsum; 1ITV; -.
PDBsum; 1L6J; -.
PDBsum; 1LKG; -.
PDBsum; 2OVX; -.
PDBsum; 2OVZ; -.
PDBsum; 2OW0; -.
PDBsum; 2OW1; -.
PDBsum; 2OW2; -.
PDBsum; 4H1Q; -.
PDBsum; 4H2E; -.
PDBsum; 4H3X; -.
PDBsum; 4H82; -.
PDBsum; 4HMA; -.
PDBsum; 4JIJ; -.
PDBsum; 4JQG; -.
PDBsum; 4WZV; -.
PDBsum; 4XCT; -.
PDBsum; 5CUH; -.
PDBsum; 5I12; -.
PDBsum; 5TH6; -.
PDBsum; 5TH9; -.
ProteinModelPortal; P14780; -.
SMR; P14780; -.
BioGrid; 110461; 18.
CORUM; P14780; -.
DIP; DIP-29518N; -.
IntAct; P14780; 10.
MINT; MINT-7709677; -.
STRING; 9606.ENSP00000361405; -.
BindingDB; P14780; -.
ChEMBL; CHEMBL321; -.
DrugBank; DB03683; 2-{[Formyl(Hydroxy)Amino]Methyl}-4-Methylpentanoic Acid.
DrugBank; DB05387; AE-941.
DrugBank; DB01197; Captopril.
DrugBank; DB01296; Glucosamine.
DrugBank; DB00786; Marimastat.
DrugBank; DB01017; Minocycline.
DrugBank; DB05495; PG-530742.
GuidetoPHARMACOLOGY; 1633; -.
MEROPS; M10.004; -.
iPTMnet; P14780; -.
PhosphoSitePlus; P14780; -.
UniCarbKB; P14780; -.
BioMuta; MMP9; -.
DMDM; 269849668; -.
EPD; P14780; -.
PaxDb; P14780; -.
PeptideAtlas; P14780; -.
PRIDE; P14780; -.
DNASU; 4318; -.
Ensembl; ENST00000372330; ENSP00000361405; ENSG00000100985.
GeneID; 4318; -.
KEGG; hsa:4318; -.
UCSC; uc002xqz.3; human.
CTD; 4318; -.
DisGeNET; 4318; -.
EuPathDB; HostDB:ENSG00000100985.7; -.
GeneCards; MMP9; -.
H-InvDB; HIX0015874; -.
HGNC; HGNC:7176; MMP9.
HPA; CAB000348; -.
HPA; CAB068199; -.
HPA; CAB068200; -.
HPA; CAB068201; -.
HPA; HPA001238; -.
HPA; HPA063909; -.
MalaCards; MMP9; -.
MIM; 120361; gene.
MIM; 603932; phenotype.
MIM; 613073; phenotype.
neXtProt; NX_P14780; -.
OpenTargets; ENSG00000100985; -.
Orphanet; 1040; Metaphyseal anadysplasia.
PharmGKB; PA30889; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00870000136399; -.
HOVERGEN; HBG052484; -.
InParanoid; P14780; -.
KO; K01403; -.
OMA; GFCPSER; -.
OrthoDB; EOG091G02JB; -.
PhylomeDB; P14780; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.35; 2681.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
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.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; P14780; -.
ChiTaRS; MMP9; human.
EvolutionaryTrace; P14780; -.
GeneWiki; MMP9; -.
GenomeRNAi; 4318; -.
PRO; PR:P14780; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000100985; -.
CleanEx; HS_MMP9; -.
Genevisible; P14780; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0005518; F:collagen binding; TAS:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; IDA:CAFA.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:CAFA.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
GO; GO:0030225; P:macrophage differentiation; TAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
GO; GO:2001258; P:negative regulation of cation channel activity; IDA:UniProtKB.
GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:CACAO.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:CACAO.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0001503; P:ossification; IEA:InterPro.
GO; GO:0030335; P:positive regulation of cell migration; TAS:ParkinsonsUK-UCL.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:CACAO.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:CACAO.
GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:CACAO.
GO; GO:1900122; P:positive regulation of receptor binding; IDA:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:CACAO.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
CDD; cd00062; FN2; 3.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.10.10.10; -; 3.
Gene3D; 2.110.10.10; -; 2.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000562; FN_type2_col-bd.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR013806; Kringle-like.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR028688; MMP9.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
PANTHER; PTHR10201:SF181; PTHR10201:SF181; 1.
Pfam; PF00040; fn2; 3.
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; SM00059; FN2; 3.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
SUPFAM; SSF57440; SSF57440; 3.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00023; FN2_1; 3.
PROSITE; PS51092; FN2_2; 3.
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; Disulfide bond; Extracellular matrix;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism;
Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 19 {ECO:0000269|PubMed:1371271,
ECO:0000269|PubMed:1400481,
ECO:0000269|PubMed:1464361,
ECO:0000269|PubMed:1653055,
ECO:0000269|PubMed:2551898,
ECO:0000269|PubMed:7669817}.
PROPEP 20 93 Activation peptide.
/FTId=PRO_0000028754.
CHAIN 94 ? 67 kDa matrix metalloproteinase-9.
/FTId=PRO_0000028755.
CHAIN 107 707 82 kDa matrix metalloproteinase-9.
/FTId=PRO_0000028756.
PROPEP ? 707 Removed in 64 kDa matrix
metalloproteinase-9 and 67 kDa matrix
metalloproteinase-9.
/FTId=PRO_0000028757.
DOMAIN 225 273 Fibronectin type-II 1.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 283 331 Fibronectin type-II 2.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 342 390 Fibronectin type-II 3.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 518 563 Hemopexin 1.
REPEAT 564 608 Hemopexin 2.
REPEAT 610 657 Hemopexin 3.
REPEAT 658 704 Hemopexin 4.
MOTIF 97 104 Cysteine switch. {ECO:0000250}.
ACT_SITE 402 402
METAL 99 99 Zinc 2; in inhibited form.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
METAL 131 131 Calcium 1.
METAL 165 165 Calcium 2; via carbonyl oxygen.
METAL 175 175 Zinc 1; structural.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
METAL 177 177 Zinc 1; structural.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
METAL 182 182 Calcium 3.
METAL 183 183 Calcium 3; via carbonyl oxygen.
METAL 185 185 Calcium 3; via carbonyl oxygen.
METAL 187 187 Calcium 3; via carbonyl oxygen.
METAL 190 190 Zinc 1; structural.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
METAL 197 197 Calcium 2; via carbonyl oxygen.
METAL 199 199 Calcium 2; via carbonyl oxygen.
METAL 201 201 Calcium 2.
METAL 203 203 Zinc 1; structural.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
METAL 205 205 Calcium 3.
METAL 206 206 Calcium 1.
METAL 208 208 Calcium 1.
METAL 208 208 Calcium 3.
METAL 401 401 Zinc 2; catalytic.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
METAL 405 405 Zinc 2; catalytic.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
METAL 411 411 Zinc 2; catalytic.
{ECO:0000269|PubMed:12051944,
ECO:0000269|PubMed:12077439}.
SITE 59 60 Cleavage; by MMP3.
SITE 106 107 Cleavage; by MMP3.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 127 127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 230 256 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 244 271 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 288 314 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 302 329 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 347 373 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 361 388 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 516 704
VARIANT 20 20 A -> V (in dbSNP:rs1805088).
{ECO:0000269|PubMed:10598806,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_013780.
VARIANT 38 38 N -> S (in dbSNP:rs41427445).
/FTId=VAR_037004.
VARIANT 82 82 E -> K (in dbSNP:rs1805089).
{ECO:0000269|PubMed:10598806}.
/FTId=VAR_013781.
VARIANT 127 127 N -> K (in dbSNP:rs3918252).
{ECO:0000269|Ref.4}.
/FTId=VAR_020054.
VARIANT 239 239 R -> H (in dbSNP:rs28763886).
{ECO:0000269|Ref.5}.
/FTId=VAR_025165.
VARIANT 279 279 Q -> R (common polymorphism; may be
associated with susceptibility to IDD;
dbSNP:rs17576).
{ECO:0000269|PubMed:10598806,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2551898,
ECO:0000269|Ref.4}.
/FTId=VAR_013782.
VARIANT 571 571 F -> V (in dbSNP:rs35691798).
{ECO:0000269|Ref.5}.
/FTId=VAR_025166.
VARIANT 574 574 R -> P (in dbSNP:rs2250889).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2551898,
ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_024595.
VARIANT 668 668 R -> Q (in dbSNP:rs17577).
{ECO:0000269|Ref.4, ECO:0000269|Ref.5}.
/FTId=VAR_014742.
MUTAGEN 402 402 E->Q: Loss of activity.
{ECO:0000269|PubMed:12051944}.
CONFLICT 110 110 F -> L (in Ref. 3; BAG35956).
{ECO:0000305}.
HELIX 42 51 {ECO:0000244|PDB:5TH6}.
HELIX 54 57 {ECO:0000244|PDB:5TH6}.
HELIX 68 78 {ECO:0000244|PDB:5TH6}.
HELIX 88 94 {ECO:0000244|PDB:5TH6}.
STRAND 103 105 {ECO:0000244|PDB:5TH6}.
STRAND 112 115 {ECO:0000244|PDB:4JIJ}.
STRAND 117 125 {ECO:0000244|PDB:4XCT}.
STRAND 130 132 {ECO:0000244|PDB:4WZV}.
HELIX 134 149 {ECO:0000244|PDB:4XCT}.
STRAND 151 153 {ECO:0000244|PDB:4WZV}.
STRAND 155 158 {ECO:0000244|PDB:4XCT}.
STRAND 160 162 {ECO:0000244|PDB:4JIJ}.
STRAND 165 171 {ECO:0000244|PDB:4XCT}.
STRAND 176 178 {ECO:0000244|PDB:4XCT}.
STRAND 183 186 {ECO:0000244|PDB:4XCT}.
STRAND 189 191 {ECO:0000244|PDB:4XCT}.
STRAND 194 196 {ECO:0000244|PDB:4XCT}.
TURN 197 200 {ECO:0000244|PDB:4XCT}.
STRAND 202 205 {ECO:0000244|PDB:4XCT}.
STRAND 213 216 {ECO:0000244|PDB:4XCT}.
STRAND 221 225 {ECO:0000244|PDB:1L6J}.
STRAND 232 238 {ECO:0000244|PDB:1L6J}.
STRAND 240 243 {ECO:0000244|PDB:1L6J}.
STRAND 255 261 {ECO:0000244|PDB:1L6J}.
HELIX 262 265 {ECO:0000244|PDB:1L6J}.
STRAND 268 270 {ECO:0000244|PDB:1L6J}.
TURN 274 276 {ECO:0000244|PDB:1L6J}.
STRAND 279 283 {ECO:0000244|PDB:1L6J}.
STRAND 290 294 {ECO:0000244|PDB:1L6J}.
STRAND 297 301 {ECO:0000244|PDB:1L6J}.
STRAND 313 319 {ECO:0000244|PDB:1L6J}.
HELIX 320 323 {ECO:0000244|PDB:1L6J}.
STRAND 326 328 {ECO:0000244|PDB:1L6J}.
HELIX 333 335 {ECO:0000244|PDB:1L6J}.
TURN 340 344 {ECO:0000244|PDB:1L6J}.
STRAND 349 353 {ECO:0000244|PDB:1L6J}.
STRAND 356 358 {ECO:0000244|PDB:1L6J}.
STRAND 372 378 {ECO:0000244|PDB:1L6J}.
HELIX 379 382 {ECO:0000244|PDB:1L6J}.
STRAND 385 387 {ECO:0000244|PDB:1L6J}.
STRAND 392 394 {ECO:0000244|PDB:4XCT}.
HELIX 395 406 {ECO:0000244|PDB:4XCT}.
STRAND 408 411 {ECO:0000244|PDB:4H3X}.
STRAND 420 422 {ECO:0000244|PDB:4XCT}.
HELIX 433 443 {ECO:0000244|PDB:4XCT}.
STRAND 444 446 {ECO:0000244|PDB:4H2E}.
HELIX 450 460 {ECO:0000244|PDB:4H3X}.
HELIX 515 517 {ECO:0000244|PDB:1ITV}.
STRAND 522 527 {ECO:0000244|PDB:1ITV}.
STRAND 530 535 {ECO:0000244|PDB:1ITV}.
STRAND 538 542 {ECO:0000244|PDB:1ITV}.
STRAND 545 547 {ECO:0000244|PDB:1ITV}.
STRAND 551 555 {ECO:0000244|PDB:1ITV}.
HELIX 556 559 {ECO:0000244|PDB:1ITV}.
STRAND 568 572 {ECO:0000244|PDB:1ITV}.
TURN 574 576 {ECO:0000244|PDB:1ITV}.
STRAND 579 583 {ECO:0000244|PDB:1ITV}.
STRAND 586 591 {ECO:0000244|PDB:1ITV}.
STRAND 594 600 {ECO:0000244|PDB:1ITV}.
HELIX 601 604 {ECO:0000244|PDB:1ITV}.
STRAND 615 618 {ECO:0000244|PDB:1ITV}.
STRAND 623 628 {ECO:0000244|PDB:1ITV}.
STRAND 631 636 {ECO:0000244|PDB:1ITV}.
TURN 637 640 {ECO:0000244|PDB:1ITV}.
HELIX 644 646 {ECO:0000244|PDB:1ITV}.
HELIX 650 653 {ECO:0000244|PDB:1ITV}.
STRAND 662 667 {ECO:0000244|PDB:1ITV}.
STRAND 670 675 {ECO:0000244|PDB:1ITV}.
STRAND 678 683 {ECO:0000244|PDB:1ITV}.
STRAND 690 696 {ECO:0000244|PDB:1ITV}.
TURN 697 700 {ECO:0000244|PDB:1ITV}.
SEQUENCE 707 AA; 78458 MW; 2165AC8CA1466209 CRC64;
MSLWQPLVLV LLVLGCCFAA PRQRQSTLVL FPGDLRTNLT DRQLAEEYLY RYGYTRVAEM
RGESKSLGPA LLLLQKQLSL PETGELDSAT LKAMRTPRCG VPDLGRFQTF EGDLKWHHHN
ITYWIQNYSE DLPRAVIDDA FARAFALWSA VTPLTFTRVY SRDADIVIQF GVAEHGDGYP
FDGKDGLLAH AFPPGPGIQG DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS
YSACTTDGRS DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS
ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP FTFLGKEYST
CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY
PMYRFTEGPP LHKDDVNGIR HLYGPRPEPE PRPPTTTTPQ PTAPPTVCPT GPPTVHPSER
PTAGPTGPPS AGPTGPPTAG PSTATTVPLS PVDDACNVNI FDAIAEIGNQ LYLFKDGKYW
RFSEGRGSRP QGPFLIADKW PALPRKLDSV FEERLSKKLF FFSGRQVWVY TGASVLGPRR
LDKLGLGADV AQVTGALRSG RGKMLLFSGR RLWRFDVKAQ MVDPRSASEV DRMFPGVPLD
THDVFQYREK AYFCQDRFYW RVSSRSELNQ VDQVGYVTYD ILQCPED


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U0553c CLIA 92 kDa gelatinase,92 kDa type IV collagenase,Canis familiaris,Canis lupus familiaris,Dog,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
E0553c ELISA kit 92 kDa gelatinase,92 kDa type IV collagenase,Canis familiaris,Canis lupus familiaris,Dog,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
E0553c ELISA 92 kDa gelatinase,92 kDa type IV collagenase,Canis familiaris,Canis lupus familiaris,Dog,Gelatinase B,GELB,Matrix metalloproteinase-9,MMP9,MMP-9 96T
15-288-21116 72 kDa type IV collagenase - EC 3.4.24.24; 72 kDa gelatinase; Matrix metalloproteinase-2; MMP-2; Gelatinase A; TBE-1 Polyclonal 0.05 mg
15-288-21116 72 kDa type IV collagenase - EC 3.4.24.24; 72 kDa gelatinase; Matrix metalloproteinase-2; MMP-2; Gelatinase A; TBE-1 Polyclonal 0.1 mg
18-003-42982 72 kDa type IV collagenase - EC 3.4.24.24; 72 kDa gelatinase; Matrix metalloproteinase-2; MMP-2; Gelatinase A; TBE-1 Polyclonal 0.1 mg Protein A
E0100r ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Rat,Rattus norvegicus 96T
U0100m CLIA 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T
E0100m ELISA kit 72 kDa gelatinase,72 kDa type IV collagenase,Gelatinase A,Matrix metalloproteinase-2,Mmp2,MMP-2,Mouse,Mus musculus 96T


 

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