TIMP1 Protein (AA 27-205, C-Term)
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- Target See all TIMP1 Proteins
- TIMP1 (TIMP Metallopeptidase Inhibitor 1 (TIMP1))
- Protein Type
- Recombinant
- Biological Activity
- Active
- Protein Characteristics
- AA 27-205, C-Term
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Origin
- Mouse
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Source
- HEK-293 Cells
- Application
- Western Blotting (WB)
- Purity
- > 90 % , as determined by Coomassie stained SDS-PAGE.
- Sterility
- 0.22 μm filtered
- Endotoxin Level
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Less than 1.0 EU per μg of protein as determine by the LAL method.
- Top Product
- Discover our top product TIMP1 Protein
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Comment
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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
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- 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.
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- 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.
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