大鼠MMP-2ELISA试剂盒描述：

       Type IV collagenase, 72-kDa, is officially designated as matrix metalloproteinase-2 (MMP2). It is also known as gelatinase. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown. Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the pro-peptide (cysteine switch). The structure of proMMP-2 reveals how the pro-peptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for pro-peptide stability. The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization. The standard product used in this kit is recombinant rat MMP-2, consisting of 662 amino acids with a molecular mass of 72kDa. The detected MMP-2 includes zymogen and active enzyme. ScienCell's rat MMP-2 ELISA kit was based on standard sandwich enzyme-linked immune-sorbent assay technology. Rat MMP-2-specific polyclonal antibodies are pre-coated onto 8 x 12 divisible strips. The rat specific-detection polyclonal antibodies are biotinylated. The test samples and biotinylated detection antibodies are subsequently added to the wells and then washed with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changes to yellow after adding acidic stop solution. The intensity of yellow is proportional to the amount of rat MMP-2 in the sample that is captured on the strips.

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       2. Morgunova, E.; Tuuttila, A.; Bergmann, U.; Isupov, M.; Lindqvist, Y.; Schneider, G.; Tryggvason, K. Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Science 284: 1667-1670, 1999.