MMP-9 antibody

Principal name

MMP-9 antibody

Alternative names for MMP-9 antibody

Matrix metalloproteinase-9, MMP9, 92 kDa type IV collagenase, 92 kDa gelatinase, GELB, Gelatinase B, CLG4B

SwissProt ID

P14780 (Human), P41245 (Mouse), P41246 (Rabit), P50282 (Rat), P52176 (Bovin)

Gene ID

4318 (MMP9), 17395 (Mmp9), 81687

Available reactivities

GP (Guinea Pig), Hu (Human), Ms (Mouse), Bov (Bovine), Can (Canine), Chk (Chicken), Por (Porcine), Rb (Rabbit), Rt (Rat), Ze (Zebrafish), African clawed frog, Marmoset, Hst (Hamster), Mky (Monkey)

Available hosts

Rabbit, Mouse, Sheep, Goat

Available applications

Immunocytochemistry/Immunofluorescence (ICC/IF), Paraffin Sections (P), Western blot / Immunoblot (WB), Enzyme Immunoassay (E), Frozen Sections (C), Immunoprecipitation (IP)

Background of MMP-9 antibody

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade extracellular matrix proteins . They are secreted as zymogens (Pro-MMPs) that are activated by a variety of proteinases or by reaction with organic mercurials. They are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs) and by 2-macroglobulin . The regulation of MMP activity is important in tissue remodeling, inflammation, tumor growth and metastasis .

Human MMP-9 (also known as gelatinase B) is secreted as a 92 kDa zymogen . Cleavage of Pro-MMP-9 at or near residue 87 results in the active enzyme with a mass of approximately 82 kDa . MMP-9 has three fibronectin type II domains, a hemopexin-like domain and a proline-rich type V collagen-homologous domain . Pro-MMP-9 can be activated by MMP-3 or by certain bacterial proteinases . MMP-9 is inhibited by.2-macroglobulin or by TIMP-1 , which binds to Pro-MMP-9 as well as to active MMP-9 . In vitro treatment of Pro-MMP-9 with 4-aminophenylmercuric acid (APMA) produces not only the 82 kDa active enzyme but also a C-terminal truncated form of approximately 65 kDa with the activity comparable to that of the 82 kDa form .

Pro-MMP-9 is secreted by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, chondrocytes, skeletal muscle satellite cells, endothelial cells, and various tumor cells(1, 7- 21). Pro-MMP-9 expression is upregulated by TGF-.1, IL-1., TGF-., PDGF-AB, TNF-., and IL-1. . Substrates for MMP-9 include denatured collagen type I (gelatin), native collagens type IV, V, VII, X and XI, fibrinogen, vitronectin, IL-1., and entactin, a molecule that bridges laminin and type IV collagen .

General readings

Wilhelm, S.M. et al. (1989) J. Biol. Chem. 264:17213.

Matrisian, L.M. (1992) BioEssays 14:455.

Birkedal-Hansen, H. et al. (1993) Crit. Rev. Oral Biol. Med. 4:197.

Birkedal-Hansen, H. (1995) Curr. Opin. Cell Biol. 7:728.

Ogata, Y. et al. (1992) J. Biol. Chem. 267:3581.

Sires, U.I. et al. (1993) J. Biol. Chem. 268:2069.

Lyons, J.G. et al. (1993) J. Biol. Chem. 268:19143.

Okada, Y. et al. (1995) Lab. Invest. 72:311.

Tamura, T. et al. (1996) Endocrinology 137:3729.

Okamoto, T. et al. (1997) J. Biol. Chem. 272:6059.

O’Connell, J.P. et al. (1994) J. Biol. Chem. 269:14967.

Koide, H. et al. (1996) Am. J. Kidney Dis. 28:32.

Hirose, T. et al. (1992) J. Rheumatol. 19:593.

Iwata, H. et al. (1996) Jpn. J. Cancer Res. 87:602.

Cullen, B. et al. (1997) Int. J. Biochem. Cell Biol. 29:241.

Guerin, C.W. and P.C. Holland (1995) Dev. Dyn. 202:91.

Hanemaaijer, R. et al. (1993) Biochem. J. 296:803.

Maeda, A. and R.A. Sobel (1996) J. Neuropathol. Exp. Neurol. 55:300.

Gress, T.M. et al. (1995) Int. J. Cancer 62:407.

Ueda, Y. et al. (1996) Am. J. Pathol. 148:611.

Lyons, J.G. et al. (1991) Biochemistry 30:1449.

Imai, K. et al. (1994) FEBS Lett. 369:249.

Ito, A. et al. (1996) J. Biol. Chem. 271:14657.

2 Item(s)

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Proteins & Growth Factors

Catalog No. Species Pres. Purity Source  

MMP-9

  Recombinant protein of human matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) (MMP9)  
MMP-9 Human > 80 %
Preparation: Recombint protein was captured through anti-DDK affinity column followed by conventiol chromatography steps.
Purity Detail: > 80% as determined by SDS-PAGE and Coomassie blue staining.
HEK293 cells
20 µg / €680.00
  OriGene Technologies, Inc.

MMP-9

  Purified recombinant protein of Mouse matrix metallopeptidase 9 (Mmp9)  
MMP-9 Mouse > 90 %
Preparation: .
Purity Detail: >90%, as determined by Coomassie stained SDS-PAGE.
HEK293 cells
10 µg / €156.00
  OriGene Technologies, Inc.

2 Item(s)

per page
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