protein

Recombinant Human Matrix metalloproteinase-9

MBS717602

0.05 mg (Yeast)

185 USD

Recombinant Protein

Recombinant Human Matrix metalloproteinase-9

Matrix metalloproteinase-9

92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB

matrix metalloproteinase-9 preproprotein; Matrix metalloproteinase-9; matrix metalloproteinase-9; matrix metallopeptidase 9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB

MMP9

MMP9; MMP9; GELB; CLG4B; MMP-9; MANDP2; CLG4B; MMP-9; GELB

MMP9_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

107-707

707

FQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAF
ALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGK
DGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFG
NADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANY
DTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSA
CTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGG
NSAGELCVFPFTFLGKEYSTC

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Developmental Biology

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.

SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages.Wilhelm S.M., Collier I.E., Marmer B.L., Eisen A.Z., Grant G.A., Goldberg G.I.J. Biol. Chem. 264:17213-17221(1989) 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.Huhtala P., Tuuttila A., Chow L.T., Lohi J., Keski-Oja J., Tryggvason K.J. Biol. Chem. 266:16485-16490(1991) Complete sequencing and characterization of 21,243 full-length human cDNAs.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.Nat. Genet. 36:40-45(2004) SeattleSNPs variation discovery resourceNIEHS SNPs programThe DNA sequence and comparative analysis of human chromosome 20.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.Nature 414:865-871(2001) Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells.Sato H., Seiki M.Oncogene 8:395-405(1993) Human neutrophil gelatinase a marker for circulating blood neutrophils. Purification and quantitation by enzyme linked immunosorbent assay.Kjeldsen L., Bjerrum O.W., Hovgaard D., Johnsen A.H., Sehested M., Borregaard N.Eur. J. Haematol. 49:180-191(1992) The cytokine-protease connection identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers.van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F., Auwerx J., van Damme J., Opdenakker G.Cytokine 3:231-239(1991) Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9.Ogata Y., Enghild J.J., Nagase H.J. Biol. Chem. 267:3581-3584(1992) Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties.Okada Y., Gonoji Y., Naka K., Tomita K., Nakanishi I., Iwata K., Yamashita K., Hayakawa T.J. Biol. Chem. 267:21712-21719(1992) Proteolytic and non-proteolytic activation of human neutrophil progelatinase B.Sang Q.X., Birkedal-Hansen H., Van Wart H.E.Biochim. Biophys. Acta 1251:99-108(1995) Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8.Masure S., Proost P., van Damme J., Opdenakker G.Eur. J. Biochem. 198:391-398(1991) Cytokine-mediated regulation of human leukocyte gelatinases and role in arthritis.Opdenakker G., Masure S., Grillet B., Van Damme J.Lymphokine Cytokine Res. 10:317-324(1991) Latent collagenase and gelatinase from human neutrophils and their activation.Tschesche H., Knaeuper V., Kraemer S., Michaelis J., Oberhoff R., Reinke H.Matrix Suppl. 1:245-255(1992) Purification and characterization of human 92-kDa type IV collagenase (gelatinase B) .Kang K., Lee D.-H.Exp. Mol. Med. 28:161-165(1996) Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1.Olson M.W., Bernardo M.M., Pietila M., Gervasi D.C., Toth M., Kotra L.P., Massova I., Mobashery S., Fridman R.J. Biol. Chem. 275:2661-2668(2000) Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease.Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F., Oppenheim F.G.Infect. Immun. 69:1402-1408(2001) Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases.Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y., Seiki M., Sato H.Oncogene 22:4617-4626(2003) Extracellular matrix protein 1 inhibits the activity of matrix metalloproteinase 9 through high-affinity protein/protein interactions.Fujimoto N., Terlizzi J., Aho S., Brittingham R., Fertala A., Oyama N., McGrath J.A., Uitto J.Exp. Dermatol. 15:300-307(2006) A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation.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.Am. J. Hum. Genet. 82:1122-1129(2008) Mutations in MMP9 and MMP13 determine the mode of inheritance and the clinical spectrum of metaphyseal anadysplasia.Lausch E., Keppler R., Hilbert K., Cormier-Daire V., Nikkel S., Nishimura G., Unger S., Spranger J., Superti-Furga A., Zabel B.Am. J. Hum. Genet. 85:168-178(2009) The adenomatous polyposis coli-associated exchange factors Asef and Asef2 are required for adenoma formation in Apc(Min/+) mice.Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M., Ohwada S., Akiyama T.EMBO Rep. 10:1355-1362(2009) Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase.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.Acta Crystallogr. D 58:1182-1192(2002) Crystal structure of human MMP9 in complex with a reverse hydroxamate inhibitor.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.J. Mol. Biol. 319:173-181(2002) Structural basis of the adaptive molecular recognition by MMP9.Cha H., Kopetzki E., Huber R., Lanzendoerfer M., Brandstetter H.J. Mol. Biol. 320:1065-1079(2002) Theoretical model of human type IV collagenase precursor.Mallena S.C., Sagajkar R.D.Submitted (APR-2002) to the PDB data bankGenetic variation at the matrix metalloproteinase-9 locus on chromosome 20q12.2-13.1.Zhang B., Henney A., Eriksson P., Hamsten A., Watkins H., Ye S.Hum. Genet. 105:418-423(1999) +Additional computationally mapped references. p>Provides general information on the entry.

74272287

NP_004985.2

NM_004994.2

P14780

68.6kD

AGE/RAGE Pathway (698754); Activation Of Matrix Metalloproteinases Pathway (1270258); Angiogenesis Pathway (198772); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (1270247); Axon Guidance Pathway (1270303); Bladder Cancer Pathway (83115); Bladder Cancer Pathway (527); CXCR4-mediated Signaling Events Pathway (137910); Collagen Degradation Pathway (1270259); Collagen Formation Pathway (1270245)

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]

MMP9: 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. 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. Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Produced by normal alveolar macrophages and granulocytes. Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Belongs to the peptidase M10A family. Protein type: Protease; Secreted; EC 3.4.24.35; Motility/polarity/chemotaxis; Secreted, signal peptide. Chromosomal Location of Human Ortholog: 20q13.12. Cellular Component: extracellular region; extracellular space; proteinaceous extracellular matrix. Molecular Function: collagen binding; endopeptidase activity; identical protein binding; metalloendopeptidase activity; metallopeptidase activity; protein binding; zinc ion binding. Biological Process: axon guidance; collagen catabolic process; embryo implantation; ephrin receptor signaling pathway; extracellular matrix disassembly; extracellular matrix organization and biogenesis; leukocyte migration; macrophage differentiation; negative regulation of apoptosis; ossification; positive regulation of DNA binding; positive regulation of epidermal growth factor receptor signaling pathway; positive regulation of keratinocyte migration; positive regulation of protein amino acid phosphorylation; proteolysis; skeletal development. Disease: Metaphyseal Anadysplasia 2

0.05 mg (Yeast)

185 USD

0.2 mg (Yeast)

420

0.05 mg (Baculovirus)

985

0.5 mg (E-Coli)

985

1 mg (E-Coli)

1170