CRIK Antibody (A-6): sc-398095

CRIK Antibody (A-6) is a mouse monoclonal IgG1 antibody that detects CRIK in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). CRIK, also known as Citron Rho-interacting kinase, is a vital 2,027 amino acid cytoplasmic protein that plays a crucial role in the regulation of cytokinesis and the development of the central nervous system. CRIK is characterized by its complex structure, which includes an AGC-kinase C-terminal domain, a CNH domain, a PH domain, a phorbol-ester/DAG-type zinc finger, and a protein kinase domain, all of which contribute to its functional versatility. The structural integrity of CRIK is essential for its interaction with other proteins, such as KIF14, which is necessary for the proper localization of KIF14 to the central spindle and midbody during cell division. Multiple alternatively spliced isoforms of CRIK, encoded by a gene located on chromosome 12q24.23, further highlight CRIK′s adaptability and importance in various cellular processes. Anti-CRIK antibody (A-6) is an invaluable tool for researchers aiming to explore the intricate roles of CRIK in cellular dynamics and its implications in developmental biology and disease.

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CRIK Antibody (A-6) References:

1. Rho-dependent transfer of Citron-kinase to the cleavage furrow of dividing cells.  |  Eda, M., et al. 2001. J Cell Sci. 114: 3273-84. PMID: 11591816
2. Citron kinase, a Rho-dependent kinase, induces di-phosphorylation of regulatory light chain of myosin II.  |  Yamashiro, S., et al. 2003. Mol Biol Cell. 14: 1745-56. PMID: 12802051
3. Negative control of keratinocyte differentiation by Rho/CRIK signaling coupled with up-regulation of KyoT1/2 (FHL1) expression.  |  Grossi, M., et al. 2005. Proc Natl Acad Sci U S A. 102: 11313-8. PMID: 16061799
4. Citron Rho-interacting kinase mediates arsenite-induced decrease in endothelial nitric oxide synthase activity by increasing phosphorylation at threonine 497: Mechanism underlying arsenite-induced vascular dysfunction.  |  Seo, J., et al. 2016. Free Radic Biol Med. 90: 133-44. PMID: 26593676
5. Citron Rho-interacting kinase silencing causes cytokinesis failure and reduces tumor growth in multiple myeloma.  |  Sahin, I., et al. 2019. Blood Adv. 3: 995-1002. PMID: 30940634
6. Prostate Cancer Progression Relies on the Mitotic Kinase Citron Kinase.  |  Rawat, C., et al. 2023. Cancer Res. 83: 4142-4160. PMID: 37801613
7. Citron Kinase Is a Druggable Target in Treatment-Resistant Prostate Cancer.  |  Mishra, R., et al. 2023. Cancer Res. 83: 4008-4009. PMID: 38098450
8. Discovery and Characterization of Selective, First-in-Class Inhibitors of Citron Kinase.  |  Maw, JJ., et al. 2024. J Med Chem. 67: 2631-2666. PMID: 38330278
9. Role of citron kinase as a target of the small GTPase Rho in cytokinesis.  |  Madaule, P., et al. 1998. Nature. 394: 491-4. PMID: 9697773
10. Citron rho-interacting kinase, a novel tissue-specific ser/thr kinase encompassing the Rho-Rac-binding protein Citron.  |  Di Cunto, F., et al. 1998. J Biol Chem. 273: 29706-11. PMID: 9792683

The preferred CRIK antibody is CRIK Antibody (E-6): sc-390437.