Matrix Metalloproteinase 2, Mouse (Mmp2, MMP-2, 72kD Type IV Collagenase, 72kD Gelatinase, Gelatinase A)
Catalog No : USB-M2420-66M
603.47€
0.00€
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| Product name | Matrix Metalloproteinase 2, Mouse (Mmp2, MMP-2, 72kD Type IV Collagenase, 72kD Gelatinase, Gelatinase A) | ||
|---|---|---|---|
| Catalog No | USB-M2420-66M | ||
| Supplier’s Catalog No | M2420-66M | ||
| Supplier | US Biologicals | ||
| Source antigen | Mouse fibroblasts | ||
| Reactivity | |||
| Cross reactivity | |||
| Applications | |||
| Molecular weight | 4042 | ||
| Storage | -70°C | ||
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| Other names | |||
| Grade | Purified | ||
| Purity | ~90% (SDS-PAGE) | ||
| Form | Supplied as a liquid in 50mM Tris-HCl, pH 7.0, 200mM sodium chloride, 5mM calcium chloride, 1uM zinc chloride, 0.05% Brij 35, 0.05% sodium azide. | ||
| Reactivity life | 12 months | ||
| Note | For reserch purpose only | ||
| Purity | ~90% (SDS-PAGE) | ||
| Description | The progelatinase A, a member of the matrix metalloproteinase (MMP) family, has been isolated from macrophages and fibroblasts. Gelatinase A hydrolyses several components of the extracellular matrix, e.g. the collagen types IV, V and XI and gelatin. Progelatinase A complexed via their C-terminal domain with TIMP-2 was isolated from culture media of different cell types. This complex shows both properties of its constituents: Like TIMP-2 it inhibits active matrix metalloproteinases and like gelatinase it shows proteolytic activity after activation with APMA (4-aminophenylmercury acetate). However, its proteolytic activity is less than 10% of that of gelatinase A not complexed with TIMP-2. In contrast to the other MMPs the progelatinase A cannot be activated by the serine proteinase trypsin. Until quite recently a potential natural activator that can transform latent progelatinase A into the active form was unknown. It was shown that the catalytic domain of the membrane type 2-matrix metalloproteinase activates progelatinase A as well as the progelatinase A/TIMP-2 complex, by cleaving the 72kD progelatinase A to yield 67kD gelatinase A, which is than transformed into 62kD gelatinase A. The 62kD form is about twice as active as the 67kD form towards the Dnp-pepitde (Masui et al.). No significant difference in activity was found between free and complexed gelatinase A forms. Source: Matrix Metalloproteinase 2, purified from mouse fibroblasts. Molecular Weight: ~40/42kD Activation: Precursor enzyme needs activation using 2mM (final concentration) aminophenylmercuric acetate (APMA) or 1mM mersalylic acid for 60-120 min. at 37°C. Do not use trypsin for activation! Do not dilute the enzyme for activation! Inhibitors: The activated enzyme is inhibited by tissue inhibitors of matrix metalloproteinase-2 (TIMP-2) and by chelators of divalent cations like EDTA or o-phenanthroline. Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. | ||
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