产品名称
磷酸化CaM激酶II抗体,α亚基,Thr286,克隆22B1, clone 22B1, Upstate®, from mouse
biological source
mouse
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)
Quality Level
Gene Information
human ... CAMK2A(815)
Analysis Note
已通过免疫印迹对大鼠脑微粒体蛋白的制剂进行常规评估
Application
可使用这种磷酸化CaM激酶II抗体(α亚基,Thr286,克隆22B1)检测磷酸化CaM激酶II,该抗体经验证可用于WB。
Biochem/physiol Actions
磷酸化CaM激酶II α亚基
General description
50kDa
Immunogen
对应于大鼠CaM激酶IIα亚基残基281-294的肽;可识别苏氨酸286处磷酸化的CaM激酶II
Physical form
形式:纯化
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
10 - Combustible liquids
wgk
WGK 1
Overexpression of calbindin-D28K in hippocampal progenitor cells increases neuronal differentiation and neurite outgrowth.
Kim, JH; Lee, JA; Song, YM; Park, CH; Hwang, SJ; Kim, YS; Kaang, BK; Son, H
Faseb Journal null
B L Patton et al.
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
Su-Ying Cui et al.
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
Comparative biology of cystic fibrosis animal models.
Fisher, JT; Zhang, Y; Engelhardt, JF
Methods in Molecular Biology null
Mar Cuadrado-Tejedor et al.
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
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