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

N° du produit ABIN2666720

Cette protéine Recombinant TIMP2 est produite dans HEK-293 Cells.

Aperçu rapide pour TIMP2 Protein (AA 27-220, C-Term) (ABIN2666720)

Antigène: TIMP2 (Metalloproteinase Inhibitor 2 (TIMP2))

Type de proteíne: Recombinant

Activité biologique: Active

Origine: Humain

Source: HEK-293 Cells

Application: Western Blotting (WB), Immunofluorescence (IF)

Pureté: > 90 % , as determined by Coomassie stained SDS-PAGE.

Détail du produit

Attributs du protein: AA 27-220, 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.

Information d'application

Indications d'application: Optimal working dilution should be determined by the investigator.

Commentaires:

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

Stockage

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.

Détail du antigène

Antigène: TIMP2 (Metalloproteinase Inhibitor 2 (TIMP2))

Autre désignation: TIMP-2

Sujet: 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.

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.

Pathways: cAMP Metabolic Process