MMP9 Antibody / Matrix metalloproteinase-9

Immunohistochemistry (FFPE): 1-2ug/ml

Optimal dilution of the antibody should be determined by the researcher.

The matrix metalloproteinases (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. 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 down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Purified

0.2 mg/ml with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide

A recombinant human partial protein (amino acids 22-166) was used as the immunogen for this MMP9 antibody.

This MMP9 antibody is available for research use only.

Cytoplasmic, nuclear, secreted

Protein G affinity chromatography

Human

P14780