Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine . Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection . May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response . During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage . Also required for p53/TP53-mediated apoptosis, phosphorylating ''Ser-392'' of p53/TP53 following UV irradiation . Phosphorylates a number of DNA repair proteins in response to DNA damage, such as MDC1, MRE11, RAD9A, RAD51 and HTATSF1, promoting their recruitment to DNA damage sites . Can also negatively regulate apoptosis . Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 . Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 . Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis . Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV . Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB . Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function . Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 . Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 . Acts as an ectokinase that phosphorylates several extracellular proteins . During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV . Phosphorylates PML at ''Ser-565'' and primes it for ubiquitin-mediated degradation . Plays an important role in the circadian clock function by phosphorylating BMAL1 at ''Ser-90'' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (By similarity). Phosphorylates CCAR2 at ''Thr-454'' in gastric carcinoma tissue . Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment . May phosphorylate histone H2A on ''Ser-1'' . .

Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1),CSNK2A1 CK2A1

P68400,Q60737,P19139

1457/12995/116549

Human,Mouse,Rat

WB,IHC,IF,ICC,ELISA

WB 1:500-2000
IHC 1:50-300
IF 1:50-200
ICC 1:50-200
ELISA 1:10000

Phospho-Casein Kinase IIα (Y255) Polyclonal Antibody detects endogenous levels of Casein Kinase IIα protein only when phosphorylated at Y255.

45kDa

Rabbit

Synthesized peptide derived from human Casein Kinase II alpha around the phosphorylation site of Tyr255.

Polyclonal

Rabbit,IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% New type preservative N.

1 mg/ml

Store at -20℃. Stable for 12 months from date of receipt.