TIMP2 Protein (AA 27-220, C-Term)

Catalog No. ABIN2666720

Product Details

Target: TIMP2 (Metalloproteinase Inhibitor 2 (TIMP2))

Protein Type: Recombinant

Biological Activity: Active

Protein Characteristics: AA 27-220, C-Term

Origin: Human

Source: HEK-293 Cells

Application: Western Blotting (WB), Immunofluorescence (IF)

Purity: > 90 % , as determined by Coomassie stained SDS-PAGE.

Sterility: 0.22 μm filtered

Endotoxin Level:

Less than 1.0 EU per μg of protein as determine by the LAL method.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

Biological activity: Human TIMP-2 inhibits the activity of activated mouse MMP-9 (100 ng/mL). The is IC50 ≤ 34 ng/mL.

Restrictions: For Research Use only

Handling

Format: Liquid

Reconstitution: For maximum results, quick spin vial prior to opening.

Buffer: 0.22 μm filtered protein solution is in 20 mM Tris, 150 mM NaCl, pH 8.0.

Handling Advice: Avoid repeated freeze/thaw cycles.

Storage: -20 °C

Storage Comment: Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for three months, or at -70°C for six months.

Target Details

Target: TIMP2 (Metalloproteinase Inhibitor 2 (TIMP2))

Alternative Name: TIMP-2 (TIMP2 Products)

Synonyms: CSC-21K Protein, DDC8 Protein, timp2l Protein, zgc:65967 Protein, zgc:85799 Protein, D11Bwg1104e Protein, Timp-2 Protein, TIMP-2 Protein, etID32613.12 Protein, fa96h09 Protein, timp2 Protein, wu:fa96h09 Protein, zgc:136726 Protein, TIMP metallopeptidase inhibitor 2 Protein, TIMP metallopeptidase inhibitor 2b Protein, tissue inhibitor of metalloproteinase 2 Protein, TIMP metallopeptidase inhibitor 2a Protein, TIMP metallopeptidase inhibitor 2 L homeolog Protein, TIMP2 Protein, timp2b Protein, Timp2 Protein, timp2a Protein, timp2.L Protein

Background: TIMPs (Tissue inhibitors of metalloproteinases) are endogenous inhibitors for MMPs (matrix metalloproteinases). The human TIMPs consist of structurally and functionally distinct N- and C-terminal domains, each of which is stabilized by three disulfide bonds. The N-terminal domain binds to the active site of MMPs, inhibiting their proteolytic activities. The bidentate coordination of the zinc ion in the active site of an MMP by the N-terminal α-amino group and carbonyl group of the Cys residue in the "cysteine switch" motif is a key mechanism of inhibition with MMPs. The C-terminal domain is known to bind hemopexin-like domain of pro-MMPs. TIMPs are broad-spectrum inhibitors of MMPs, but there are some differences in specificity among them. Human metalloproteinase inhibitor 2 (TIMP-2) expression in melanocytes is regulated by MITF. Besides inhibitory functions, TIMP-2 also has erythroid potentiating and cell growth promoting activities. Interestingly, TIMP-2-deficient mice demonstrated increased tumor growth, enhanced expression of angiogenic marker αvβ3 in tumor and endothelial cells, and significantly higher serum vascular endothelial growth factor A levels. Tumor-bearing TIMP-2 -/- mice showed a significant number of inflammatory cells in their tumors, upregulation of inflammation mediators, nuclear factor-κB, and Annexin A1 as well as higher levels of serum IL-6. TIMP-2 is widely expressed in many mammalian tissues, notably in the reproductive organs. TIMP-2 is able to promote cell proliferation in a wide range of cell types and may also have an anti-apoptotic function. It has anti-angiogenic activity by preventing endothelial cell migration.

Molecular Weight: Predicted molecular mass of approximately 22 kDa. The protein migrates at about 25 kDa in DTT-reducing conditions and about 22 kDa in non-reducing condition by SDS-PAGE. The N-terminal amino acid is Cys.

Pathways: cAMP Metabolic Process