A synthetic peptide corresponding to amino acids 603-614 of human MMP-9
Alternative Names:
82 kDa matrix metalloproteinase-9, 92 kDa type IV collagenase, CLG 4B, CLG4B, Collagenase Type 4 beta, Collagenase type IV 92 KD, EC 3.4.24.35, Gelatinase 92 KD, Gelatinase B, Gelatinase beta, GELB, Macrophage gelatinase, MANDP2,
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. Primary antibodies are available purified, or with a selection of fluorescent CF Dyes and other labels. CF Dyes offer exceptional brightness and photostability. Note: Conjugates of blue fluorescent dyes like CF405S and CF405M are not recommended for detecting low abundance targets, because blue dyes have lower fluorescence and can give higher non-specific background than other dye colors.
