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

Recombinant TIMP1-Protein exprimiert in HEK-293 Cells.
Produktnummer ABIN2666718

Kurzübersicht für TIMP1 Protein (AA 27-205, C-Term) (ABIN2666718)

Target

Alle TIMP1 Proteine anzeigen
TIMP1 (TIMP Metallopeptidase Inhibitor 1 (TIMP1))

Protein-Typ

Recombinant

Biologische Aktivität

Active

Spezies

  • 13
  • 11
  • 3
  • 3
  • 3
  • 3
  • 3
  • 2
  • 2
  • 1
  • 1
Maus

Quelle

  • 20
  • 9
  • 8
  • 3
  • 2
  • 1
  • 1
  • 1
HEK-293 Cells

Applikation

Western Blotting (WB)

Reinheit

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

    AA 27-205, C-Term

    Sterilität

    0.22 μm filtered

    Endotoxin-Niveau

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

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  • Applikationshinweise

    Optimal working dilution should be determined by the investigator.

    Kommentare

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

    Beschränkungen

    Nur für Forschungszwecke einsetzbar
  • Format

    Liquid

    Rekonstitution

    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.

    Handhabung

    Avoid repeated freeze/thaw cycles.

    Lagerung

    -20 °C

    Informationen zur Lagerung

    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

    TIMP1 (TIMP Metallopeptidase Inhibitor 1 (TIMP1))

    Andere Bezeichnung

    TIMP-1

    Hintergrund

    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.

    Molekulargewicht

    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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