Tissue Inhibitor of Metalloproteinases 2 (TIMP Metallopeptidase Inhibitor 2, TIMP2, TIMP-2, CSC-21K, Metalloproteinase Inhibitor 2)

TIMPs are members of tissue inhibitor of matrix metalloproteinases (MMPs). There are four member in the family, TIMP1, TIMP2, TIMP3, and TIMP4. The main function of TIMPs is their inhibitory effect on MMPs. TIMPs irreversibly inactivate MMPs by direct binding to their catalytic zinc cofactor and resultant inhibition of proteinase function (1,2). In addition to MMP inhibition,\nTIMP members have also been shown to interact with varying membrane receptors on the cell surface, some of these interactions include: TIMP1 with CD63, TIMP2 with a3b1 integrin, and TIMP3 with VEGFR2, all of which result in distinct cellular effects (3). TIMPs have been shown\ninvolved in a wide variety of biological functions, such as tumor angiogenesis and progression (4,5), wound healing, and vascular remodeling (6,7). Mutations of TIMP3 are associated with Sorsby

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SPECIFICATIONS

Catalog Number

T5585-28

Size

100ul

Applications

WB

Hosts

Rabbit

Reactivities

Hum, Mouse, NHP

Form

Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, less than 0.02% sodium azide, 50% glycerol.

P Type

Mab

Purity

Purified

Isotype

IgG

References

(1) Nagase, H. et al. (2006) Cardiovasc Res 69, 562-73. (2) Visse, R. and Nagase, H. (2003) Circ Res 92, 827-39. (3) Stetler-Stevenson, W.G. (2008) Sci Signal 1, re6. (4) Noel, A. et al. (2004) J Clin Pathol 57, 577-84. (5) Hojilla, C.V. et al. (2003) Br J Cancer 89, 1817-21. (6) Gill, S.E. and Parks, W.C. (2008) Int J Biochem Cell Biol 40, 1334-47. (7) Raffetto, J.D. and Khalil, R.A. (2008) Biochem Pharmacol 75, 346-59.\n(8) Weber, B.H. et al. (1994) Nat Genet 8, 352-6. (9) Yeow, K.M. et al. (2002) Matrix Biol 21, 75-88.

Additional Info

Recognizes endogenous levels of total TIMP2. Species Crossreactivity: monkey, mouse.