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目录号:A5743
特异性 | ILK Rabbit Recombinant mAb detects endogenous levels of total ILK. |
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背景 | Integrin-linked kinase (ILK) is a serine/threonine kinase. ILK can anchor to integrins by interacting with the cytoplasmic domain of certain β integrin subunits. ILK localizes to both focal adhesions and fibrillar adhesion. It has a low basal kinase activity, which is stimulated transiently by cell–ECM interactions and by certain growth factors. The activity is stimulated in a phosphatidylinositol (PI) 3-kinase–dependent manner and likely involves binding of the phosphoinositide phospholipid product of PI 3-kinase, PI 3,4,5-triphosphate, to the PH-like domain of ILK. ILK activity is regulated negatively by two phosphatases: PTEN, a tumor suppressor lipid phosphatase, which dephosphorylates PI 3,4,5-triphosphate to PI 4,5-bisphosphate, and a PP2C protein phosphatase, ILKAP. ILK could directly phosphorylate proteins such as PKB (PKB/Akt) on ser 473, glycogen synthase kinase 3 (GSK-3) on ser 9, myosin light chain (MLC) on ser 18/thr 19, and ILK-binding protein affixin. In addition, ILK can phosphorylate the cytoplasmic domain of β1 integrin subunit in vitro. It is concluded that ILK plays a central role in connecting integrins to actin filaments, and it also plays crucial roles in the regulation of cell survival, cell proliferation, and cell-cell adhesion. |
抗体应用 | wb,ELISA,ELISA | ||
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稀释比例 |
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反应性 | Human Mouse Rat | ||
MW (kDa) | 51kDa | ||
抗体类型 | |||
储存液配方 | 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. | ||
储存条件 (自收到货起) |
Store at –20°C. |
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WB
Validated by Selleck