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Mouse Anti-CSNK2A1 Recombinant Antibody (14e23) (CBMAB-C3017-LY)

This product is antibody recognizes CSNK2A1. The antibody 14e23 immunoassay techniques such as: ELISA, IHC, IP, WB.
See all CSNK2A1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
14e23
Antibody Isotype
IgG2a, κ
Application
ELISA, IHC, IP, WB

Basic Information

Immunogen
Recombinant protein corresponding to human CSNK2A1 expressed in E. coli (His-Casein kinase II a)
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
CSNK2A1
Introduction
CSNK2A1 (Casein Kinase 2 Alpha 1) is a Protein Coding gene. Diseases associated with CSNK2A1 include Okur-Chung Neurodevelopmental Syndrome and Cardiomyopathy, Dilated, 1P. Among its related pathways are Mitotic Prometaphase and Mitophagy - animal. Gene Ontology (GO) annotations related to this gene include transferase activity, transferring phosphorus-containing groups and protein tyrosine kinase activity.
An important paralog of this gene is CSNK2A3.
Entrez Gene ID
UniProt ID
Alternative Names
Casein Kinase 2 Alpha 1; Casein Kinase 2, Alpha 1 Polypeptide; EC 2.7.11.1; CK2A1; Casein Kinase II Alpha 1 Polypeptide Pseudogene; Casein Kinase II Alpha 1 Subunit; Casein Kinase II Subunit Alpha; CK2 Catalytic Subunit Alpha; Protein Kinase CK2;
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 (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621, PubMed:24962073).

Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (PubMed:12631575, PubMed:19387552, PubMed:19387551).

May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (PubMed:12631575, PubMed:19387552, PubMed:19387551).

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 (PubMed:11704824, PubMed:19188443).

Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis (PubMed:11239457).

Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:16193064).

Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:16193064).

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 (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551, PubMed:23123191).

Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (PubMed:19387550).

Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (PubMed:30699359).

Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (PubMed:19387549).

Acts as an ectokinase that phosphorylates several extracellular proteins (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551).

During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551).

Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (PubMed:20625391, PubMed:22406621).

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 (By similarity).

Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073).
Biological Process
Apoptotic process Source: UniProtKB-KW
Chaperone-mediated protein folding Source: UniProtKB
Macroautophagy Source: Reactome
Mitotic chromosome condensation Source: Reactome
Negative regulation of apoptotic signaling pathway Source: ARUK-UCL
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Negative regulation of ubiquitin-dependent protein catabolic process Source: ARUK-UCL
Peptidyl-serine phosphorylation Source: UniProtKB
Peptidyl-threonine phosphorylation Source: CAFA
Phosphatidylcholine biosynthetic process Source: Reactome
Positive regulation of cell growth Source: UniProtKB
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of protein catabolic process Source: UniProtKB
Positive regulation of Wnt signaling pathway Source: UniProtKB
Protein folding Source: Reactome
Protein phosphorylation Source: UniProtKB
Regulation of cell cycle Source: GO_Central
Regulation of chromosome separation Source: UniProtKB
Regulation of signal transduction by p53 class mediator Source: Reactome
Rhythmic process Source: UniProtKB-KW
Signal transduction Source: ProtInc
Wnt signaling pathway Source: UniProtKB-KW
Cellular Location
Nucleus
Involvement in disease
Okur-Chung neurodevelopmental syndrome (OCNDS):
An autosomal dominant neurodevelopmental disorder characterized by developmental delay, intellectual disability, behavioral problems, hypotonia, speech problems, microcephaly, pachygyria and variable dysmorphic features.
PTM
Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase. Phosphorylation does not directly affect casein kinase 2 activity, but may contribute to its regulation by forming binding sites for interacting proteins and/or targeting it to different compartments.
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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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