MyBioSource.com's CSNK2A2 Antibody is a Rabbit Polyclonal antibody. This antibody has been shown to work in applications such as: ELISA, Immunohistochemistry, and Western Blot. The CSNK2A2 Antibody was generated using CSNK2A2 as the antigen and it reacts with Human, Mouse, and Rat.
Description
Description: Casein kinase I (also designated CKI) and casein kinase II (CKII) compose a family of serine/threonine protein kinases which are present in all eukaryotes examined to date. Casein kinase I family members, which include casein kinase I?, I?, I? and Ie, have been implicated in the control of cytoplasmic and nuclear processes, including DNA replication and repair. CKII is usually expressed as a tetrameric complex consisting of either an ?2ˆ«2 or an ??'ˆ«2 structure. The a catalytic subunit is stimulated by the ˆ« regulatory subunit, which undergoes autophosphorylation. Casein kinase II activity is high in the cytosol and nucleus of proliferating and differentiating cells. Casein kinase II is known to phosphorylate more than 100 different substrates including nuclear oncoproteins, transcription factors and enzymes involved in DNA metabolism.
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.
Subunit Structure: Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1.
Similarity: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily