MMP2; MMP-2; CLG4; CLG4A; Matrix metallopeptidase 2; 72 kDa Type IV collagenase precursor; 72 kDa gelatinase, Gelatinase A
ELISA, Western Blot, Immunohistochemistry
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-2 (also designated type IV collagenase) cleaves Collagen Types IV, V, VII and X and gelatin type I. Activation of MMP-2 secretion requires the Ras signaling pathway.
Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the C-terminus of the human MMP2 protein and mouse myeloma Ag8563 cells.
Oesophageal and gastric tissues. Expression higher cancerous tissue versus normal tissues.
Provided as solution in phosphate buffered saline with 0.08% sodium azide
Product should be stored at -20ºC. Aliquot to avoid freeze/thaw cycles
1. Talvensaari-Mattila, A., et al. (2005). Prognostic value of matrix metalloproteinase-2 (MMP-2) expression in endometrial endometrioid adenocarcinoma. Anticancer Res. 25(6B);4101-4105.2. Honkavuori, M., et al. (2007). MMP-2 expression associates with CA125 and clinical course in endometrial carcinoma. Gynecol. Oncol. 104(1);217-221.