CaMKII-α Antibody [P6K24] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Lane 1: Mouse brain, Lane 2: Rat brain

Usage Information

Dilution
WB1:400-1:2000 IHC1:2000

Application
WB, IHC

Reactivity
Mouse, Rat, Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
54 kDa 100 kDa, 50-70 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Human brain tissue; Rat brain tissue; Mouse brain tissue; Rat normal brain (Purkinje cells, cerebellum)
Negative Control

Datasheet & SDS

Biological Description

Specificity
CaMKII-α Antibody [P6K24] detects endogenous levels of total CaMKII-α protein.

Clone
P6K24

Synonym(s)
CAMKA; KIAA0968; CAMK2A; Calcium/calmodulin-dependent protein kinase type II subunit alpha; CaM kinase II subunit alpha; CaMK-II subunit alpha

Background
CaMKII-α (calcium/calmodulin-dependent protein kinase II alpha) is the principal neuronal isoform of the CaMKII serine/threonine kinase family and assembles into dodecameric or tetradecameric holoenzymes that are pivotal for synaptic plasticity and memory formation. CaMKII-α contains an N-terminal bilobal kinase domain (residues 1-270) where conserved Asp156 and Lys42 coordinate ATP in the catalytic cleft, an autoinhibitory regulatory domain (271-315) with a pseudosubstrate sequence in which Arg-to-Thr286 mimics substrate occlusion and blocks access until displaced by Ca²⁺/calmodulin (CaM), a variable linker region that allows for flexible kinase positioning, and a C-terminal hub/association domain (316-478) that forms a rigid toroidal β-sheet scaffold via four-helix bundles per subunit, supporting intersubunit allosteric interactions. Upon Ca²⁺/CaM binding, the regulatory domain is displaced, relieving autoinhibition and exposing Thr286 for intersubunit trans-autophosphorylation, which prevents CaM dissociation (the "CaM trap") and confers Ca²⁺-independent activity that can persist for over an hour. This mechanism enables CaMKII-α to decode Ca²⁺ oscillation frequency by sequential, wave-like phosphorylation that propagates bidirectionally around the holoenzyme ring, amplifying signaling events such as GluA1 Ser831 phosphorylation to drive AMPAR trafficking and long-term potentiation (LTP). Autophosphorylation at Thr305/306 or oxidation (Met281/282 sulfenic acid formation) further modulates autoinhibition recapture, while phosphatases PP1 and PP2A reverse Thr286 phosphorylation, a process that can be inhibited by PKA crosstalk. Pathologically, hyperactivity of α-CaMKII due to T286I mutation or SCN1A-linked disinhibition leads to epilepsy through hyperexcitable neuronal networks and dendritic defects; heterozygous knockout impairs hippocampal LTP and spatial memory, but can confer resilience to neurodegeneration. Additionally, isoform imbalance disrupts CaV1.2 channel coupling, contributing to cardiac arrhythmias.

Background

CaMKII-α (calcium/calmodulin-dependent protein kinase II alpha) is the principal neuronal isoform of the CaMKII serine/threonine kinase family and assembles into dodecameric or tetradecameric holoenzymes that are pivotal for synaptic plasticity and memory formation. CaMKII-α contains an N-terminal bilobal kinase domain (residues 1-270) where conserved Asp156 and Lys42 coordinate ATP in the catalytic cleft, an autoinhibitory regulatory domain (271-315) with a pseudosubstrate sequence in which Arg-to-Thr286 mimics substrate occlusion and blocks access until displaced by Ca²⁺/calmodulin (CaM), a variable linker region that allows for flexible kinase positioning, and a C-terminal hub/association domain (316-478) that forms a rigid toroidal β-sheet scaffold via four-helix bundles per subunit, supporting intersubunit allosteric interactions. Upon Ca²⁺/CaM binding, the regulatory domain is displaced, relieving autoinhibition and exposing Thr286 for intersubunit trans-autophosphorylation, which prevents CaM dissociation (the "CaM trap") and confers Ca²⁺-independent activity that can persist for over an hour. This mechanism enables CaMKII-α to decode Ca²⁺ oscillation frequency by sequential, wave-like phosphorylation that propagates bidirectionally around the holoenzyme ring, amplifying signaling events such as GluA1 Ser831 phosphorylation to drive AMPAR trafficking and long-term potentiation (LTP). Autophosphorylation at Thr305/306 or oxidation (Met281/282 sulfenic acid formation) further modulates autoinhibition recapture, while phosphatases PP1 and PP2A reverse Thr286 phosphorylation, a process that can be inhibited by PKA crosstalk. Pathologically, hyperactivity of α-CaMKII due to T286I mutation or SCN1A-linked disinhibition leads to epilepsy through hyperexcitable neuronal networks and dendritic defects; heterozygous knockout impairs hippocampal LTP and spatial memory, but can confer resilience to neurodegeneration. Additionally, isoform imbalance disrupts CaV1.2 channel coupling, contributing to cardiac arrhythmias.

References
https://pubmed.ncbi.nlm.nih.gov/11931644/ https://pubmed.ncbi.nlm.nih.gov/20668654/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%