Human Matrix Metalloproteinease-2 (72 kDa Type IV Collagenase) ELISA KitIHUMMP2KT
This Human Matrix Metalloproteinease-2 (72 kDa Type IV Collagenase) ELISA Kit from Innovative Research is intended for quantitative detection of human MMP-2 in cell culture supernates, serum and plasma (heparin). Strip well format. Reagents for up to 96 tests.
This human MMP-2 ELISA Kit was based on standard sandwich enzyme-linked immune-sorbent assay technology. A monoclonal antibody from mouse specific for MMP-2 has been precoated onto 96-well plates. Standards(NSO, A30-C660) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for MMP-2 is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex was added and unbound conjugates were washed away with PBS or TBS buffer. HRP substrate TMB was used to visualize HRP enzymatic reaction. TMB was catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the human MMP-2 amount of sample captured in plate.
- Detection Target: Matrix Metalloproteinease-2 (72 kDa Type IV Collagenase)
- Uniprot ID: P08253)
- Reactivity: Human
- Cross-Reactivity: There is no detectable cross-reactivity with other relevant proteins.
- Range: 625pg/ml-40000pg/ml
- Sensitivity: <10pg/ml
- Storage Conditions: Store at 4?C for 6 months, at -20?C for 12 months. Avoid multiple freeze-thaw cycles. (Shipped with wet ice)
Additional Information: The capture antibody is a monoclonal antibody from mouse, the detection antibody is a biotinylated polyclonal antibody from goat. Expression system for standard: Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2(MMP2). It is also known as gelatinase, 72-kD. 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 propeptide(cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability. The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization. The standard product used in this kit is recombinant human MMP-2, consisting of 631 amino acids with the molecular mass of 71KDa. The detected MMP-2 includes zymogen and active enzyme.; Immunogen sequence: 380
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