||Recombinant Human TIMP2 is expressed in Sf9 cells. TIMP-2 shows a protein band with a molecular weight of 21-kDa (nonreduced) or 24-kDa (reduced) on SDS-polyacrylamide gel electrophoresis.
||The tissue Inhibitor of Metalloproteinases (TIMP) belongs to a family which takes part in the activation and regulation of the MMP-activity: TIMP-1, a 28-kDa glycoprotein; TIMP-2, a 21-kDa glycoprotein and the N-glycosylated TIMP-3 (27-kDa, reduced SDS-PAGE). TIMP-4 is thought to function in a tissue-specific fashion in the ECM hemostasis. These proteins are expressed in a variety of cell types and form with latent as well as with active MMPs non-covalent, stoichiometric complexes. Progelatinase B and the activated gelatinase B specifically bind TIMP-1 via their C-terminal domain. Purified TIMP-2 inhibits the activities of stromelysin 1 (MMP-3), matrilysin (MMP-7), gelatinase A (MMP-2) and the interstitial collagenase (MMP-1).On the MMP-2 the TIMP displays two distinct binding sites.
||Liquid, in 50 mM Tris-HCl, pH 7; 200 mM NaCl, 5 mM CaCl2, 1 μM ZnCl2, 0.05% Brij 35, 0.05% NaN3.
||homogenous by electrophoresis and western blotting analysis.
||It is recommended to perform a pre-incubation of about 20 min 37°C which allows the formation of the enzyme-inhibitor complex.
|Stability And Storage:
||The protein can be kept stored at -70°C for month, at -20°C for several weeks and at 4°C for 1 week without significant loss of inhibitory activity. Repeated freezing and thawing must be avoided.