CSNK2A1 antibody - 100 µg
Host : Rabbit
Clonality: Polyclonal
Clone:
Isotype: IgG
Immunogen: casein kinase 2, alpha 1 polypeptide
Purity: ≥95% as determined by SDS-PAGE
Form: Liquid
Molecular weight: 45 kDa
Uniprot: P68400
Gene id: 1457
Background: 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).
Field of research: Cell Division and Proliferation, Signal Transduction, Metabolism
Storage conditions: PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months(Avoid repeated freeze
thaw cycles.)
Applications: ELISA, WB, IHC, IF, IP
Dilution: WB: 1:500-1:2000; IP: 1:500-1:2000; IHC: 1:20-1:200; IF: 1:10-1:100
Target: CSNK2A1
Purification: Immunogen affinity purified
Reactivity: Human, Mouse, Rat
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Clonality: Polyclonal
Clone:
Isotype: IgG
Immunogen: casein kinase 2, alpha 1 polypeptide
Purity: ≥95% as determined by SDS-PAGE
Form: Liquid
Molecular weight: 45 kDa
Uniprot: P68400
Gene id: 1457
Background: 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).
Field of research: Cell Division and Proliferation, Signal Transduction, Metabolism
Storage conditions: PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months(Avoid repeated freeze
thaw cycles.)
Applications: ELISA, WB, IHC, IF, IP
Dilution: WB: 1:500-1:2000; IP: 1:500-1:2000; IHC: 1:20-1:200; IF: 1:10-1:100
Target: CSNK2A1
Purification: Immunogen affinity purified
Reactivity: Human, Mouse, Rat