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.
Formulation
1 mg/ml in 1X PBS; BSA free, sodium azide free
Host
Mouse
Immunogen Region
Amino acids 603-614 were used as the immunogen for the Matrix metalloproteinase 9 antibody.
Isotype
Mouse IgG1, kappa
Species Reactivity
Human
Note
Optimal dilution of the antibody should be determined by the researcher.
Uniprot
P14780
Format
Purified
Purity
Protein G affinity chromatography
Storage
Store the Matrix metalloproteinase 9 antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).