|Application ||WB, IHC-P, E|
|Other Accession||P28020, P19139, P33674, Q60737, P21868, P68399|
|Reactivity||Human, Mouse, Rat|
|Predicted||Bovine, Chicken, Rabbit, Xenopus|
|Calculated MW||45144 Da|
|Antigen Region||240-269 aa|
|Other Names||Casein kinase II subunit alpha, CK II alpha, CSNK2A1, CK2A1|
|Target/Specificity||This CKII alpha (CSNK2A1) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 240-269 amino acids from the Central region of human CKII alpha (CSNK2A1).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CKII alpha (CSNK2A1) Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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. 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. 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, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. 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 ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073).|
|Tissue Location||Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level).|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation.
Miyata, Y., et al., Mol. Cell. Biol. 24(9):4065-4074 (2004).
Loizou, J.I., et al., Cell 117(1):17-28 (2004).
Filhol, O., et al., EMBO Rep. 5(4):351-355 (2004).
Kulartz, M., et al., Biochem. Biophys. Res. Commun. 315(4):1011-1017 (2004).
Sachs, N.A., et al., J. Neurochem. 88(1):51-62 (2004).
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