Western Blot, Immunohistochemistry(paraffin sections)
Protein A/G Chromatography
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.
Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the N-terminus of the human MMP9 protein and mouse myeloma Ag8563 cells. Sequence common in rabbit, dog and pig
Esophageal adenocarcinoma. Only present in tumor tissues.
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Left: Immunohistochemical staining of paraffin embedded esophageal tumors using Act-MMP9 antibody (Cat. No. X2057M).Right: Western blot using MMP9 antibody on recombinant human proenzyme MMP9 (left lane) and activated enzyme (right lane).
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