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

Protéine Recombinant TIMP1 exprimée dans HEK-293 Cells.
N° du produit ABIN2666718

Aperçu rapide pour TIMP1 Protein (AA 27-205, C-Term) (ABIN2666718)

Antigène

Voir toutes TIMP1 Protéines
TIMP1 (TIMP Metallopeptidase Inhibitor 1 (TIMP1))

Type de proteíne

Recombinant

Activité biologique

Active

Origine

  • 13
  • 12
  • 4
  • 4
  • 4
  • 4
  • 3
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
Souris

Source

  • 19
  • 17
  • 8
  • 3
  • 2
  • 1
  • 1
  • 1
HEK-293 Cells

Application

Western Blotting (WB)

Pureté

> 90 % , as determined by Coomassie stained SDS-PAGE.
  • Attributs du protein

    AA 27-205, C-Term

    Stérilité

    0.22 μm filtered

    niveau d'endotoxine

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

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  • Indications d'application

    Optimal working dilution should be determined by the investigator.

    Commentaires

    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.

    Conseil sur la manipulation

    Avoid repeated freeze/thaw cycles.

    Stock

    -20 °C

    Stockage commentaire

    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.
  • Antigène

    TIMP1 (TIMP Metallopeptidase Inhibitor 1 (TIMP1))

    Autre désignation

    TIMP-1

    Sujet

    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.

    Poids moléculaire

    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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