MMP-9 Mouse Monoclonal Antibody [2G3]

Function

The matrix metallo proteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc (3). MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is downregulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Background References

1. Gu, T.T., et al. 2012. Cytoplasmic NANOG-positive stromal cells promote human cervical cancer progression. Am. J. Pathol. 181: 652-661.

2. Mathalone, N., et al. 2011. MMP expression in leaking filtering blebs and tears after glaucoma filtering surgery. Graefes Arch. Clin. Exp. Ophthalmol. 249: 1047-1055.

3. Bendinelli, P., et al. 2011. Comparative role of acetylation along c-SRC/ETS1 signaling pathway in bone metastatic and invasive mammary cell phenotypes. Biochim. Biophys. Acta 1813: 1767-1776.

Subcellular Location

Secreted

UNIPROT

SwissProt: P14780 Human

Synonyms