TIMP Metallopeptidase Inhibitor 1 (TIMP1) (AA 27-205), (C-Term) (Active) Protein

Details for Product No. ABIN2666718, Supplier: Log in to see
Protein Name
  • TIMP-1
  • TIMP1
  • DKFZp468A0912
  • CLGI
  • EPA
  • EPO
  • HCI
  • TIMP
  • Timp
  • Clgi
  • TIMP metallopeptidase inhibitor 1
  • tissue inhibitor of metalloproteinase 1
  • TIMP1
  • Timp1
  • LOC100009047
Protein Characteristics
AA 27-205, C-Term
18
5
5
2
2
1
1
1
1
1
1
1
1
1
Origin
Mouse (Murine)
31
7
6
2
2
2
2
1
1
1
1
Source
HEK-293
27
8
6
5
5
3
2
1
1
1
1
Protein Type
Recombinant
Biological Activity
Active
Application
Western Blotting (WB)
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Available images

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.

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.
Research Area Extracellular Matrix, Cancer, Inflammation
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
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.
Supplier Images
ELISA image for TIMP Metallopeptidase Inhibitor 1 (TIMP1) (AA 27-205), (C-Term) (Active) Protein (ABIN2666718) TIMP Metallopeptidase Inhibitor 1 (TIMP1) (AA 27-205), (C-Term) (Active) protein
Background publications Murphy: "Tissue inhibitors of metalloproteinases." in: Genome biology, Vol. 12, Issue 11, pp. 233, 2012 (PubMed).

Kim, Kim, Kang, Ko: "Expression level and glycan dynamics determine the net effects of TIMP-1 on cancer progression." in: BMB reports, Vol. 45, Issue 11, pp. 623-8, 2012 (PubMed).

Brew, Nagase: "The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity." in: Biochimica et biophysica acta, Vol. 1803, Issue 1, pp. 55-71, 2010 (PubMed).

Bourboulia, Stetler-Stevenson: "Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion." in: Seminars in cancer biology, Vol. 20, Issue 3, pp. 161-8, 2010 (PubMed).