Anti-ILK (b1-Integrin-Linked Kinase):
Marker for integrin-mediated processes

Cell adhesion to the extracellular matrix (ECM) is an important process that controls cell morphology, proliferation, migration, differentiation and survival. Transduction of ECM signals through integrins influences intracellular and extracellular functions and appears to require interaction of integrin cytoplasmic domains with cellular proteins.

The gene that interacts with the cytoplasmic domain of b1-integrin and b3-integrin subunits is a ubiquitously expressed 50-59 kDa serine/threonine protein kinase designated integrin-linked kinase (ILK). ILK has been implicated in integrin, growth factor and Wnt signaling pathways [1-3]. This kinase regulates several integrin-mediated cellular processes including cell adhesion, fibronectin matrix assembly and anchorage-dependent cell progression [1,4,5]. ILK is localized to cell-matrix focal adhesions, but not in cell-cell adhesion sites [6]. Upon cell adhesion, ILK is transiently activated [7]. Overexpression of ILK in epithelial cells activates the LEF-1/ b -catenin signaling pathways and inhibits the E-cadherin pathway [4,8].

Insulin transiently stimulates ILK activity in cells through a phosphatidylinositol 3-kinase (PI3-kinase)-dependent mechanism. ILK directly phosphorylates PKB/Akt and glycogen synthase kinase-3 (GSK3) and regulates their activities [4]. In addition, ILK plays critical roles in the regulation of cellular survival and proliferation and may be involved in oncogenic transformation.

Anti-ILK (Prod. No. I 1907) is produced using a peptide corresponding to amino acids 435-452 at the C-terminus of human ILK. The peptide sequence is identical in mouse, guinea-pig and chicken ILK-1 and is highly conserved (single amino acid substitution) in human ILK-2 and in Drosophila ILK (>80% homology). Anti-ILK specifically recognizes human, mouse, rat and chicken ILK (50 kDa). This antibody is suitable for immunoblotting and immunofluorescence.

References:

1. Hannigan, G.E., et al., Nature, 379, 91-96 (1996).
2. Li, F., et al., Biochim. Biophys. Acta, 1358, 215-220 (1997).
3. Wu, C. and Dedhar, S., J. Cell Biol., 155, 505-510 (2001).
4. Wu, C., et al., J. Biol. Chem., 273, 528-536 (1998).
5. Radeva, G., et al., J. Biol. Chem., 272, 13937-13944 (1997).
6. Li, F., et al., J. Cell Sci., 112, 4589-4599 (1999).
7. Delcommenne, M., et al., Proc. Natl. Acad. Sci. USA, 95, 11211-11216 (1998).
8. Novak, A., et al., Proc. Natl. Acad. Sci. USA, 95, 4374-4379 (1998).

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