Anti-Integrin linked ILK Antibody Picoband® (Dylight488 Conjugate)

ILK, also known as Integrin-linked kinase, is a serine-threonine protein kinase. Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK) interacts with the cytoplasmic domain of beta-1 integrin. This gene was initially described to encode a serine/ threonine protein kinase with 4 ankyrin-like repeats, which associates with the cytoplasmic domain of beta integrins and acts as a proximal receptor kinase regulating integrin-mediated signal transduction. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. Recent results showed that ILK contains 5 ankyrin-like repeats, and that the C-terminal kinase domain is actually a pseudo-kinase with adaptor function.

The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.

Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity). .

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.

Western blot, 0.1-0.25 μg/ml, Human, Mouse, Rat<br> Immunohistochemistry(Paraffin-embedded Section), 2-5 μg/ml, Human, Mouse, Rat<br> Immunocytochemistry/Immunofluorescence, 5 μg/ml, Human<br> Flow Cytometry (Fixed), 1-3 μg/1x10⁶ cells, Human, Mouse, Rat<br> ELISA, 0.1-0.5 μg/ml, -<br>