Prokaryotic recombinant protein corresponding to a 134 amino acid portion of the C-terminal region of the mature human MMP9 molecule
Alternative Synonym:
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 (MMPs) are a family of zinc containing enzymes involved in the degradation of different components of the extracellular matrix and tissue remodelling. MMPs, which are expressed widely during growth and development, have been classified into collagenases, gelatinases and stromelysins, based on the in vitro substrate specificity. More recently several MMPs have been identified as membrane-type specific and matrilysin families. MMPs are multidomain proteins and are secreted as inactive precursors, which are activated by cleavage of an N-terminal pro-peptide. The major natural inhibitors of MMPs are tissue inhibitors of matrix metalloproteinases (TIMPs) which complex with MMPs and are involved in regulating the activity and activation of individual MMPs. MMP9 degrades collagen type IV, a major component of extracellular matrix. MMP9 is also reported to be observed immunohistochemically in normal kidney tubules, hepatocytes, spermatids, myocytes, stomach parietal cells, prostatic columnar epithelium and uterine cells.
200ug/ml of Ab produced in CHO cell mammalian-based expression system. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
SDS-PAGE Analysis of Purified Matrix Metalloproteinase 9 (MMP9) Recombinant Mouse Monoclonal Antibody (r15W2). Confirmation of Purity and Integrity of Antibody.
Formalin-fixed, paraffin-embedded human spleen stained with Matrix Metalloproteinase 9 (MMP9) Recombinant Mouse Monoclonal Antibody (r15W2). Inset: PBS instead of primary antibody, secondary only negative control.
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