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I0783

Sigma-Aldrich

Monoclonal Anti-ILK antibody produced in mouse

~2 mg/mL, clone 65.1, purified immunoglobulin, buffered aqueous solution

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Synonym(s):
Anti-Integrin-linked protein kinase
MDL number:
MFCD01633545
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

65.1, monoclonal

form

buffered aqueous solution

mol wt

antigen ~59 kDa

species reactivity

rat, human, bovine, monkey, mouse, canine

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
microarray: suitable
western blot: 0.5-2.0 μg/mL using whole cell extract of Chinese hamster ovary cell line (CHO cells)

isotype

IgG2b

UniProt accession no.

Q13418

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ILK(3611)
mouse ... Ilk(16202)
rat ... Ilk(170922)

General description

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).

Immunogen

purified mouse ILK recombinant protein.

Application

Monoclonal Anti-ILK antibody produced in mouse has been used in:
  • immunostaining
  • immunoprecipitation
  • immunocytochemistry
  • immunohistochemistry
  • western blotting

Biochem/physiol Actions

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.

Physical form

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

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Regulatory Information

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Promoter characterization and genomic organization of the gene encoding integrin-linked kinase 1
Melchior C, et al.
Biochimica et Biophysica Acta (BBA)-Gene Structure and Expression, 1575(1-3), 117-122 (2002)
Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
Wu C and Dedhar S
The Journal of Cell Biology, 155(4), 505-510 (2001)
Requirement for integrin-linked kinase in neural crest migration and differentiation and outflow tract morphogenesis
Dai X, et al.
BMC Biology, 11(1), 107-107 (2013)
Pinch1 is required for normal development of cranial and cardiac neural crest-derived structures
Liang X, et al.
Circulation Research, 100(4), 527-535 (2007)
Kindlin-2 controls TGF-beta signalling and Sox9 expression to regulate chondrogenesis
Wu C, et al.
Nature Communications, 6(1), 7531-7531 (2015)
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