05-533
Anti-phospho-CaM Kinase II Antibody, α subunit, (Thr286), clone 22B1
clone 22B1, Upstate®, from mouse
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Anti-Anti-CAMKA, Anti-Anti-CaMKIINalpha, Anti-Anti-CaMKIIalpha, Anti-Anti-MRD53, Anti-Anti-MRT63
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biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
22B1, monoclonal
species reactivity
rat
manufacturer/tradename
Upstate®
technique(s)
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
phosphorylation (pThr286)
Gene Information
human ... CAMK2A(815)
Specificity
phospho-CaM Kinase II α subunit
Immunogen
Peptide corresponding to residuues 281-294 of rat Cam Kinase II alpha-subunit; recognizes phosphorylated CaM Kinase II on Threonine 286
Application
Detect phospho-CaM Kinase II using this Anti-phospho-CaM Kinase II Antibody, α subunit, (Thr286), clone 22B1 validated for use in WB.
Quality
routinely evaluated by immunoblot on rat brain microsomal protein preparation
Target description
50kDa
Physical form
Format: Purified
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
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Journal of neurochemistry, 136(3), 609-619 (2015-11-13)
The Ca(2+) modulation in the dorsal raphe nucleus (DRN) plays an important role in sleep-wake regulation. Calmodulin-dependent kinase II (CaMKII) is an important signal-transducing molecule that is activated by Ca(2+) . This study investigated the effects of intracellular Ca(2+) /CaMKII
Overexpression of calbindin-D28K in hippocampal progenitor cells increases neuronal differentiation and neurite outgrowth.
Faseb Journal null
Molecular biology of the cell, 4(2), 159-172 (1993-02-01)
We have visualized the distribution of autophosphorylated type II CaM kinase in neural tissue with the use of two complementary antibodies: a monoclonal antibody that binds to the alpha and beta subunits of the kinase only when they are autophosphorylated
Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology, 42(2), 524-539 (2016-08-24)
The targeting of two independent but synergistic enzymatic activities, histone deacetylases (HDACs, class I and HDAC6) and phosphodiesterase 5 (PDE5), has recently been validated as a potentially novel therapeutic approach for Alzheimer's disease (AD). Here we report the discovery of
Comparative biology of cystic fibrosis animal models.
Methods in Molecular Biology null
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