Anti-phospho-CaMKII beta (Ser331)

Evaluated by Western Blotting in HEK293T cells transfected with CaMKII WT or mutant S331A.

Western Blotting Analysis: A 1:500 dilution of this antibody detected phospho-CaMKII beta (Ser331) in HEK293T cells transfected with CaMKII WT, but not the mutant S331A.

Anti-phospho-CaMKII beta (Ser331), Cat. No. ABS2107, is a highly specific rabbit polyclonal antibody that targets Calcium/calmodulin-dependent protein kinase type II subunit beta (CaMK-II subunit beta) and has been tested for use in Immunocytochemistry and Western Blotting.

Western Blotting Analysis: A representative lot detected phospho-CaMKII beta (Ser331) in HEK293T cells transfected with CaMKII WT or mutants (Kim, K., et. al. (2015). Neuron. 87(4):813-26).

Immunocytochemistry Analysis: A representative lot detected phospho-CaMKII beta (Ser331) in dissociated hippocampal neurons (Kim, K., et. al. (2015). Neuron. 87(4):813-26).

This rabbit polyclonal antibody detects beta subunit of CaM Kinase II when phosphorylated on Ser331.

Calcium/calmodulin-dependent protein kinase type II subunit beta (UniProt: P08413; also known as EC: 2.7.11.17, CaM kinase II subunit beta, CaMK-II subunit beta) is encoded by the Camk2b gene (Gene ID: 24245) in rat. CaM kinase II is one of the most widely studied multi-functional enzyme. It is found in high concentrations in the brain and in some regions it may constitute up to 2% of the total protein content. CaM kinase II is a complex of about 12 subunits, which exist in four differentially expressed forms (alpha, beta, gamma, and delta). CaMKII beta contains an auto-inhibitory domain (aa 283-293), a calmodulin-binding domain (aa 291-301) and a unique C-terminal association domain responsible for oligomerization. It is activated Ca2+/calmodulin and binding of calmodulin results in conformational change that relieves intrasteric autoinhibition and allows autophosphorylation of Thr-287 which turns the kinase in a constitutively active form and confers to the kinase a Ca2+-independent activity that persists even after withdrawal of calcium. Phosphorylation of Thr-287 locks the kinase into an activated state. CaM Kinase II typically recognizes the phosphorylation site sequence Arg-X-X-Ser/Thr. It prefers arginine in the P3 position, which is reported to make an electrostatic contact with Glu96 in the catalytic core.

~60 kDa observed; 60.40 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

A linear peptide corresponding to 10 amino acids surrounding phopho serine 331 of rat CaM Kinase II beta.

Concentration: Please refer to lot specific datasheet.