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

This Recombinant TIMP2 protein is produced in HEK-293 Cells.
Catalog No. ABIN2666720

Quick Overview for TIMP2 Protein (AA 27-220, C-Term) (ABIN2666720)

Target

See all TIMP2 Proteins
TIMP2 (Metalloproteinase Inhibitor 2 (TIMP2))

Protein Type

Recombinant

Biological Activity

Active

Origin

  • 14
  • 5
  • 3
  • 3
  • 3
  • 3
  • 3
  • 2
  • 2
  • 2
  • 2
Human

Source

  • 21
  • 8
  • 7
  • 4
  • 1
  • 1
HEK-293 Cells

Application

Western Blotting (WB), Immunofluorescence (IF)

Purity

> 90 % , as determined by Coomassie stained SDS-PAGE.
  • Protein Characteristics

    AA 27-220, C-Term

    Sterility

    0.22 μm filtered

    Endotoxin Level

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

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  • 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
  • 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

    TIMP2 (Metalloproteinase Inhibitor 2 (TIMP2))

    Alternative Name

    TIMP-2

    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
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