This antibody is provided in phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide at 0.5 mg/ml.
Preparation:
This antibody was purified by affinity chromatography.
Concentration:
0.5 mg/ml
Storage & Handling:
Upon receipt, store undiluted at 4°C.
Application:
WB - Quality Tested IHC(Paraffin)1*, ELISA * - *This application has been reported in the literature.
Recommended Usage:
Each lot of this antibody is quality control tested by Western blotting. For Western blotting, suggested working dilution(s): Use 5-10 μg per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
Application References:
1. Murray, G. et al. 1998. Gut. 43:791. 2. Fromique, O., et al. 2008. J Biol Chem. 283:30549. PubMed
Western blot analysis of recombinant human TIMP-2 protein using anti-TIMP-2, clone F27P3A4.
Description:
TIMP-2 (Tissue inhibitor of metalloproteinase 2) is a nonglycosylated protein that belongs to the protease inhibitor I35 (TIMP) family. Contains 1 NTR domain, predicted molecular weight 24 kD. The mechanisms of TIMPs inhibit angiogenesis appear to be specific for each member of the TIMP family. TIMP-2 binds to the surface of human endothelial cells through interaction with the integrin α3β1, and abrogates angiogenic factor induced endothelial cell proliferation in vitro and angiogenesis in vivo independent of MMP inhibition. Clone F27P3A4 has been shown to be useful for western blotting, immunohistochemistry and ELISA of human, mouse, rabbit, chicken, zebrafish, and pig TIMP-2.
Other Names:
Metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2; TIMP2
Structure:
Belongs to the protease inhibitor I35 (TIMP) family. Contains 1 NTR domain, predicted molecular weight 24 kD.
Distribution:
Extracellular
Function:
TIMP-2 binds to the surface of human endothelial cells through interaction with the integrin α3β1, and abrogates angiogenic factor induced endothelial cell proliferation in vitro and angiogenesis in vivo independent of MMP inhibition.
Interaction:
MMP2, MMP8, MMP14, CD49C
Antigen References:
1. Stetler-Stevenson., et al. 1989. J. Biol. Chem. 264: 17374
