TIMP1 Protein (AA 27-205, C-Term)

Catalog No. ABIN2666718

Product Details

Target: TIMP1 (TIMP Metallopeptidase Inhibitor 1 (TIMP1))

Protein Type: Recombinant

Biological Activity: Active

Protein Characteristics: AA 27-205, C-Term

Origin: Mouse

Source: HEK-293 Cells

Application: Western Blotting (WB)

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: Mouse TIMP-1 inhibits the activity of activated mouse MMP-9 (100 ng/mL). The IC50 ≤ 90 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: TIMP1 (TIMP Metallopeptidase Inhibitor 1 (TIMP1))

Alternative Name: TIMP-1 (TIMP1 Products)

Synonyms: TIMP-1 Protein, TIMP1 Protein, DKFZp468A0912 Protein, CLGI Protein, EPA Protein, EPO Protein, HCI Protein, TIMP Protein, Timp Protein, Clgi Protein, TIMP metallopeptidase inhibitor 1 Protein, tissue inhibitor of metalloproteinase 1 Protein, TIMP1 Protein, Timp1 Protein

Background: TIMPs (tissue inhibitors of metalloproteinases) are endogenous inhibitors for MMPs (matrix metalloproteinases). The 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" is a key mechanism of inhibition with MMPs. The TIMP's 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. Mouse metalloproteinase inhibitor 1, TIMP-1, is more restricted in its inhibitory range than the other three TIMPs, having a relatively low affinity for the membrane-type MMPs, MMP-14, MMP-16, and MMP-24 as well as for MMP-19. Mouse TIMP-1 shares a 72 % homology with its human counterpart. It is widely expressed in many mammalian tissues, notably in the reproductive organs. TIMP-1 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. CD63 has been identified as a receptor for TIMP-1. TIMP-1 binding to CD63 inhibits apoptosis and arrests cell growth. TIMP-1-null mice exhibit a number of alterations in processes associated with reproduction, steroidogenesis and impaired learning and memory. In addition, mice deficient in TIMP-1 exhibit enhanced MMP activity that would contribute to a reduction of atherosclerotic plaque size, neverthless, it promotes aneurysm formation.

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.