Recombinant Human TIMP-2 (Recombinant Human Tissue Inhibitor of Metalloproteinases 2; rHuTIMP-2);重组人组织金属蛋白酶抑制剂2
Synonyms
CSC-21Ktissue inhibitor of metalloproteinase 2; metalloproteinase inhibitor 2; TIMP metallopeptidase inhibitor 2; TIMP-2; Tissue inhibitor of metalloproteinases 2
Purity
>95% by SDS-PAGE and HPLC analyses.
Biological Activity
Fully biologically active when compared to standard. The biologically active as determined by its ability to inhibit humanmMP-2 cleavage of a fluorogenic peptide substrate Mca-PLGL-Dpa-ARNH2.
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4, with 3% trehalose.
Endotoxin
Less than 1EU/μg of rHuTIMP-2 as determined by LAL method.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/ml. Stock solutions should be apportioned into working aliquots and stored at ≤-20℃. Further dilutions should be made in appropriate buffered solutions.
Category
Enzymes
Background
TIMPs-1 through -4 regulate the activity of zinc metalloproteases known asmMPs, ADAMs and ADAMTSs. Structurally, TIMPs contain two domains. The N-terminal domain binds to the active site of mature metalloproteases via a 1:1 non-covalent interaction, blocking access of substrates to the catalytic site. In addition, The C-terminal domain of TIMP-1 and TIMP-2 binds to the hemopexin-like domain of pro-MMP-9 and pro-MMP-2, respectively. The latter binding is essential for the cell surface activation ofmMP-2 bymMP-14.