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Human ILK Protein expressed in HEK-293 Cells - ABIN2723535
Radovanac, Morgner, Schulz, Blumbach, Patterson, Geiger, Mann, Krieg, Eckes, Fässler, Wickström: Stabilization of integrin-linked kinase by the Hsp90-CHIP axis impacts cellular force generation, migration and the fibrotic response. in The EMBO journal 2013
Targeted knockdown of the integrin focal adhesion complex components beta-integrin, PINCH (show LIMS1 Proteins), and integrin-linked kinase caused formation of multinucleate epidermal cells within the Drosophila larval epidermis.
PINCH (show LIMS1 Proteins) and ILK have an independent capacity to localize at muscle attachment sites in vivo.
ILK functions as an essential hub in the assembly of its partner proteins at sites of integrin adhesion.
We conclude that ILK is critical for maintaining the collecting duct epithelium and renal function and is a key intermediate for periostin (show POSTN Proteins) activation of signaling pathways involved in cyst growth and fibrosis in PKD (show PRKD1 Proteins).
Ilk and ELMO2 (show ELMO2 Proteins) modulate recycling endosomes in keratinocytes undergoing intercellular adhesion mediated through cell-cell contacts, including E-cadherin (show CDH1 Proteins)-based adherens junctions.
Ilk regulates cellular mechanics facilitating the motility in 3D extracellular matrices.
It was concluded that ILK depletion modifies the transcription of GLUT4 (show SLC2A4 Proteins), which results in reduced peripheral insulin (show INS Proteins) sensitivity and glucose uptake, suggesting ILK as a molecular target and a prognostic biomarker of insulin (show INS Proteins) resistance.
results demonstrate that TGF-beta1 (show TGFB1 Proteins)-induced autophagy links beta-catenin (show CTNNB1 Proteins) and Smad (show SMAD1 Proteins) signaling to promote epithelial-mesenchymal transition in C1.1 cells through a novel pY654-beta-catenin (show CTNNB1 Proteins)/p-Smad2 (show SMAD2 Proteins)/ILK pathway.
ILK deletion impaired the developmental profile, proliferation, and differentiation of oligodendrocyte precursor cells.
Our results define ILK as a key mechanotransducer in modulating breast cancer stem-like cells development in response to tissue mechanics and oxygen tension.
iNOS (show NOS2 Proteins)-derived NO plays a crucial role during atherosclerosis by regulating the endocytic-lysosomal degradation of ILK in endothelial cells.
Hepatic ILK deletion has no effect on insulin (show INS Proteins) action in lean mice but sensitizes the liver to insulin (show INS Proteins) during the challenge of high fat feeding. This effect corresponds to changes in the expression and activation of key insulin (show INS Proteins) signaling pathways as well as a greater capacity for hepatic mitochondrial glucose oxidation.
this study has identified a new role for Parvin (show PARVA Proteins) and alphaPix (show ARHGEF6 Proteins) downstream of the integrin-ILK signaling axis for mammary epithelial cell differentiation.
Heart failure in recessive embryonic lethal zebrafish mutant main squeeze (msq) mutants is due to a mutation in the integrin-linked kinase (ilk) gene.
The lost-contact mutant on chromosome 10 encodes a nonsense mutation (Y319X) associated with defective cardiomyocytes & endothelial cells that leads to severe myocardial dysfunction. There is epistatic regulation between laminin-alpha4, integrin, & Ilk.
Data show that integrin-linked kinase is an essential component downstream of laminin and integrin alpha7, providing strengthening of skeletal muscle fibre adhesion with the extracellular matrix.
ILK-induced epithelial-mesenchymal transition is a novel mechanism in the pathogenesis of adenomyosis
Herein, we propose a new ILK-MMP9 (show MMP9 Proteins)-MRTF axis that appears to be critical for endothelial-mesenchymal transition differentiation of endothelial to cancer-associated fibroblasts -like cells. Thus, it might be an attractive target for cancer treatment
The current data support MT1-MMP (show MMP14 Proteins) as an additional ILK substrate and show that modulation of ILK expression and activity inhibit MT1-MMP (show MMP14 Proteins)-related pro-metastatic behaviors of ovarian cancer cells.
Results show that ILK is overexpressed in metastasis of bladder cancer and the up-regulation of ILK could increase cell proliferation, change cell morphology and regulate cell cycle promoting epithelial-mesenchymal transition.
This study is the first to identify EMILIN-1 (show EMILIN1 Proteins) and ILK as prospective markers of islet regenerative function in human mesenchymal stem cells.
ILK aids trophoblast syncytialization via downregulation of CDH1 (show CDH1 Proteins), perhaps through an ILK-PARP1 (show PARP1 Proteins)-SNAI1 (show SNAI1 Proteins) pathway
Emodin inhibits the migration and invasion abilities of human endometrial stromal cells by by facilitating the mesenchymal-epithelial transition through targeting integrin-linked kinase.
KRAS-E2F1-ILK-hnRNPA1 regulatory loop enables pancreatic cancer cells to promote oncogenic KRAS signaling and to interact with the tumor microenvironment to promote aggressive phenotypes.
Data indicate a regulatory role for tetraspanin 8 (Tspan8 (show TSPAN8 Proteins)) in melanoma progression by modulating cell-matrix interactions through beta1 integrin - integrin-linked kinase (ILK) axis and establish Tspan8 (show TSPAN8 Proteins) as a negative regulator of ILK activity.
Integrin-linked kinase (ILK, MGC129022) is an important regulator of the endothelial phenotype and vascular network formation by directing the assembly and/or maturation of alpha5beta1-competent matrix-forming adhesions.
Rac1 only partially restores the spreading defects of integrin linked kinasse (ILK)-depleted cells, suggesting that an additional ILK-dependent signal is required for cell spreading.
Profilin (show PFN1 Proteins)-dependent dissociation of G-actin (show ACTB Proteins)-Tbeta4 complexes simultaneously liberates actin for filament assembly and facilitates Tbeta4 binding to integrin-linked kinase (ILK) in the lamellipodia.
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 encodes 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.
, Integrin-linked kinase
, integrin linked kinase
, integrin-linked protein kinase
, integrin-linked kinase
, Integrin-linked protein kinase
, integrin binding protein kinase
, main squeeze
, beta-integrin-linked kinase
, 59 kDa serine/threonine-protein kinase
, integrin-linked kinase-2