Anti-Chk1 antibody

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Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed : 11535615, PubMed : 12399544, PubMed : 12446774, PubMed : 14559997, PubMed : 14988723, PubMed : 15311285, PubMed : 15650047, PubMed : 15665856, PubMed : 32357935). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed : 11535615, PubMed : 12399544, PubMed : 12446774, PubMed : 14559997, PubMed : 14988723, PubMed : 15311285, PubMed : 15650047, PubMed : 15665856). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed : 11535615, PubMed : 12399544, PubMed : 12446774, PubMed : 14559997, PubMed : 14988723, PubMed : 15311285, PubMed : 15650047, PubMed : 15665856). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed : 11535615, PubMed : 12399544, PubMed : 12446774, PubMed : 14559997, PubMed : 14988723, PubMed : 15311285, PubMed : 15650047, PubMed : 15665856). Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed : 12676583, PubMed : 12676925, PubMed : 12759351, PubMed : 14559997, PubMed : 14681206, PubMed : 19734889, PubMed : 9278511). Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C (PubMed : 9278511). Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed : 12676583, PubMed : 12676925, PubMed : 12759351, PubMed : 14681206, PubMed : 19734889, PubMed : 9278511). Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A (PubMed : 19734889, PubMed : 20090422, PubMed : 9278511). Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed : 9278511). Also phosphorylates NEK6 (PubMed : 18728393). Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination (PubMed : 15665856). Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation (PubMed : 10673501, PubMed : 15659650, PubMed : 16511572). Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed : 17296736). Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed : 12660173, PubMed : 12955071). This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed : 12660173, PubMed : 12955071). May also play a role in replication fork maintenance through regulation of PCNA (PubMed : 18451105). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity). Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed : 17380128). Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed : 31316063). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed : 33108758).. Isoform 2. Endogenous repressor of isoform 1, interacts with, and antagonizes CHK1 to promote the S to G2/M phase transition.