Clone: 2C3
Background: 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.
Positive Control: Colon, oesophageal and gastric tissues. Stronger expression in tumor versus normal tissue.
Purification Method: Protein A/G Chromatography
Concentration: See vial for concentration
Source: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the C-terminus of the human MMP9 protein and mouse myeloma Ag8563 cells.
References: 1. Wang, L. et al. (2006). Matrix metalloproteinase 2 (MMP2) and MMP9 secreted by erythropoietin-activated endothelial cells promote neural progenitor cell migration. J. Neurosci. 26(22);5996-60032. Solmiari, S.B., et al. (2006). Circulating MMP2 and MMP9 in breast cancer -- potential role in classification of patients into low risk, high risk, benign disease and breast cancer categories. Int. J. Cancer. 119(6);1403-14113. Chen, X., et al. (2005). Increased plasma MMP9 in integrin alpha1-null mice enhances lung metastasis of colon carcinoma cells. Int. J. Cancer. 116(1);52-61
UniProt: P14780 (Human)
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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