Rabbit polyclonal primary
MMP9 Rabbit Polyclonal Antibody (ER1706-40)
Synthetic peptide within human mmp9 aa 105-179.
U937 cell lysates, Hela, MCF-7, PANC-1, human spleen tissue, mouse spleen tissue, human tonsil tissue, HL-60.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Peptide affinity purified.
82 kDa matrix metalloproteinase-9 antibody; 92 kDa gelatinase antibody; 92 kDa type IV collagenase antibody; CLG 4B antibody; CLG4B antibody; Collagenase Type 4 beta antibody; Collagenase type IV 92 KD antibody; EC 188.8.131.52 antibody; Gelatinase 92 KD antibody; Gelatinase B antibody; Gelatinase beta antibody; GelatinaseB antibody; GELB antibody; Macrophage gelatinase antibody; MANDP2 antibody; Matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) antibody; Matrix Metalloproteinase 9 antibody; MMP 9 antibody; MMP-9 antibody; MMP9 antibody; MMP9_HUMAN antibody; Type V collagenase antibody
Belongs to the peptidase M10A family.
Detected in neutrophils (at protein level). Produced by normal alveolar macrophages and granulocytes.
Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.; N- and O-glycosylated.
Extracellular matrix. Secreted.
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 downregulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.