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Mouse Anti-ILK Recombinant Antibody (17A4) (CBMAB-0639-CN)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
17A4
Antibody Isotype
IgG
Application
ELISA, MA

Basic Information

Immunogen
Recombinant full length protein of ILK
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
>95%, as determined by SDS-PAGE analysis
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
integrin-linked kinase
Introduction
Integrin-linked kinase (ILK) is an intracellular protein, which interacts with the cytoplasmic domains of integrin beta1 and beta3 subunits. The encoded protein associates at the cell membrane with the cytoplasmic domain of beta integrins, where it regulates integrin-mediated signal transduction. ILK can mediate the phosphorylation of a variety of intracellular substrates, most notable of which are: protein kinase B (PKB/Akt), glycogen synthase kinase-3 (GSK-3) and myosin light chain.
Entrez Gene ID
3611
UniProt ID
Q13418
Alternative Names
P59; ILK-1; ILK-2; p59ILK; HEL-S-28
Function
Receptor-proximal protein kinase regulating integrin-mediated signal transduction (PubMed:8538749, PubMed:9736715).
May act as a mediator of inside-out integrin signaling (PubMed:10712922).
Focal adhesion protein part of the complex ILK-PINCH (PubMed:10712922).
This complex is considered to be one of the convergence points of integrin- and growth factor-signaling pathway (PubMed:10712922).
Could be implicated in mediating cell architecture, adhesion to integrin substrates and anchorage-dependent growth in epithelial cells (PubMed:10712922).
Regulates cell motility by forming a complex with PARVB (PubMed:32528174).
Phosphorylates beta-1 and beta-3 integrin subunit on serine and threonine residues, but also AKT1 and GSK3B (PubMed:8538749, PubMed:9736715).
Biological Process
Branching involved in ureteric bud morphogenesisIEA:Ensembl
Cell morphogenesisManual Assertion Based On ExperimentIMP:ARUK-UCL
Cell projection organizationIEA:Ensembl
Cell-matrix adhesionManual Assertion Based On ExperimentIBA:GO_Central
Establishment or maintenance of epithelial cell apical/basal polarityIEA:Ensembl
Fibroblast migrationIEA:Ensembl
Integrin-mediated signaling pathwayManual Assertion Based On ExperimentIDA:MGI
Myelination in peripheral nervous systemIEA:Ensembl
Negative regulation of neural precursor cell proliferationIEA:Ensembl
Nerve developmentIEA:Ensembl
Outflow tract morphogenesisIEA:Ensembl
Peptidyl-serine phosphorylationIEA:Ensembl
Platelet aggregationManual Assertion Based On ExperimentHMP:UniProtKB
Positive regulation of BMP signaling pathwayIEA:Ensembl
Positive regulation of canonical Wnt signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of cell population proliferationIEA:Ensembl
Positive regulation of NIK/NF-kappaB signalingManual Assertion Based On ExperimentIMP:CAFA
Positive regulation of osteoblast differentiationIEA:Ensembl
Positive regulation of phosphorylationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of protein phosphorylationManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of signal transductionManual Assertion Based On ExperimentIMP:UniProtKB
Positive regulation of substrate adhesion-dependent cell spreadingManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIMP:UniProtKB
Protein kinase B signalingIEA:Ensembl
Protein phosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Substrate adhesion-dependent cell spreadingManual Assertion Based On ExperimentIMP:UniProtKB
Tumor necrosis factor-mediated signaling pathwayManual Assertion Based On ExperimentIMP:CAFA
Cellular Location
Cell membrane; Cytoplasm, myofibril, sarcomere
PTM
Autophosphorylated on serine residues.
More Infomation

Górska, A., & Mazur, A. J. (2022). Integrin-linked kinase (ILK): the known vs. the unknown and perspectives. Cellular and Molecular Life Sciences, 79(2), 100.

McDonald, P. C., & Dedhar, S. (2022). New perspectives on the role of integrin-linked kinase (ILK) signaling in cancer metastasis. Cancers, 14(13), 3209.

Martucci, N., Michalopoulos, G. K., & Mars, W. M. (2021). Integrin linked kinase (ILK) and its role in liver pathobiology. Gene Expression, 20(3), 201.

Yue, Y., Wang, C., Benedict, C., Huang, G., Truongcao, M., Roy, R., ... & Kishore, R. (2020). Interleukin-10 deficiency alters endothelial progenitor cell–derived exosome reparative effect on myocardial repair via integrin-linked kinase enrichment. Circulation research, 126(3), 315-329.

Tsirtsaki, K., & Gkretsi, V. (2020). The focal adhesion protein Integrin-Linked Kinase (ILK) as an important player in breast cancer pathogenesis. Cell Adhesion & Migration, 14(1), 204-213.

Zheng, C. C., Hu, H. F., Hong, P., Zhang, Q. H., Xu, W. W., He, Q. Y., & Li, B. (2019). Significance of integrin-linked kinase (ILK) in tumorigenesis and its potential implication as a biomarker and therapeutic target for human cancer. American journal of cancer research, 9(1), 186.

Brodehl, A., Rezazadeh, S., Williams, T., Munsie, N. M., Liedtke, D., Oh, T., ... & FORGE Canada Consortium. (2019). Mutations in ILK, encoding integrin-linked kinase, are associated with arrhythmogenic cardiomyopathy. Translational Research, 208, 15-29.

Gulzar, M., Syed, S. B., Khan, F. I., Khan, P., Ali, S., Hasan, G. M., ... & Hassan, M. I. (2019). Elucidation of interaction mechanism of ellagic acid to the integrin linked kinase. International journal of biological macromolecules, 122, 1297-1304.

Karachaliou, N., Cardona, A. F., Bracht, J. W. P., Aldeguer, E., Drozdowskyj, A., Fernandez-Bruno, M., ... & Rosell, R. (2019). Integrin-linked kinase (ILK) and src homology 2 domain-containing phosphatase 2 (SHP2): Novel targets in EGFR-mutation positive non-small cell lung cancer (NSCLC). EBioMedicine, 39, 207-214.

de Frutos, S., Luengo, A., García-Jérez, A., Hatem-Vaquero, M., Griera, M., O'Valle, F., ... & Calleros, L. (2019). Chronic kidney disease induced by an adenine rich diet upregulates integrin linked kinase (ILK) and its depletion prevents the disease progression. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1865(6), 1284-1297.

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For research use only. Not intended for any clinical use.

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