Monoclonal Anti-ILK antibody produced in mouse

Monoclonal Anti-ILK (mouse IgG2b isotype) is derived from the 65.1 hybridoma produced by the fusion of mouse myeloma cells (P3X63-Ag8.653) and splenocytes from BALB/c mice immunized with purified mouse ILK recombinant protein. Integrin-linked kinase (ILK) is a ubiquitously expressed 50-59 kDa serine/threonine kinase that has three structurally well-conserved domains. A C-terminal domain contains the kinase catalytic site as well as the binding site for integrin β1 cytoplasmic domain. A N-terminal domain contains four ankyrin repeats (ANK).

purified mouse ILK recombinant protein.

Monoclonal Anti-ILK antibody produced in mouse has been used in:

• immunostaining
• immunoprecipitation
• immunocytochemistry
• immunohistochemistry
• western blotting

Integrin-linked kinase (ILK) is a serine-threonine kinase that interacts with PINCH and parvin to modulate cell adhesion, growth, differentiation, migration and invasion. This kinase binds to integrin β1, β2 and β3 domains to regulate integrin signalling. ILK functions as a receptor-proximal effector for integrin and growth factor dependent signal transduction. ILK is associated with cell cycle progression and oncogenic transformation. The kinase activity of ILK is low in non-activated cells; its activity is stimulated by cell-extracellular matrix (ECM) interactions and by certain growth factors. Negative regulation of ILK is mediated by two phosphatases: phosphatase and tensin homolog (PTEN), a tumor suppressor lipid phosphatase and ILKAP (ILK associated serine/threonine phosphatase), a protein phosphatase 2C (PP2C) protein phosphatase. In tumor cells that do not express PTEN protein, ILK is constitutively active.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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