|Application ||WB, IHC-P, E|
|Other Accession||O77708, Q95266, Q6PHZ2|
|Predicted||Mouse, Pig, Rabbit|
|Calculated MW||56369 Da|
|Antigen Region||448-478 aa|
|Other Names||Calcium/calmodulin-dependent protein kinase type II subunit delta, CaM kinase II subunit delta, CaMK-II subunit delta, CAMK2D, CAMKD|
|Target/Specificity||This CAMK2D (CAMK2 delta) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 448-478 amino acids from the C-terminal region of human CAMK2D (CAMK2 delta).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CAMK2D (CAMK2 delta) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(2+) uptake and Na(+) and K(+) channel transport. Targets also transcription factors and signaling molecules to regulate heart function. In its activated form, is involved in the pathogenesis of dilated cardiomyopathy and heart failure. Contributes to cardiac decompensation and heart failure by regulating SR Ca(2+) release via direct phosphorylation of RYR2 Ca(2+) channel on 'Ser- 2808'. In the nucleus, phosphorylates the MEF2 repressor HDAC4, promoting its nuclear export and binding to 14-3-3 protein, and expression of MEF2 and genes involved in the hypertrophic program. Is essential for left ventricular remodeling responses to myocardial infarction. In pathological myocardial remodeling acts downstream of the beta adrenergic receptor signaling cascade to regulate key proteins involved in ECC. Regulates Ca(2+) influx to myocytes by binding and phosphorylating the L-type Ca(2+) channel subunit beta-2 CACNB2. In addition to Ca(2+) channels, can target and regulate the cardiac sarcolemmal Na(+) channel Nav1.5/SCN5A and the K+ channel Kv4.3/KCND3, which contribute to arrhythmogenesis in heart failure. Phosphorylates phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2, contributing to the enhancement of SR Ca(2+) uptake that may be important in frequency-dependent acceleration of relaxation (FDAR) and maintenance of contractile function during acidosis. May participate in the modulation of skeletal muscle function in response to exercise, by regulating SR Ca(2+) transport through phosphorylation of PLN/PLB and triadin, a ryanodine receptor- coupling factor.|
|Cellular Location||Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side|
|Tissue Location||Expressed in cardiac muscle and skeletal muscle. Isoform Delta 3, isoform Delta 2, isoform Delta 8 and isoform Delta 9 are expressed in cardiac muscle. Isoform Delta 11 is expressed in skeletal muscle.|
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Provided below are standard protocols that you may find useful for product applications.
CaM-kinase II (CAMK2) is a prominent Ser/Thr protein kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Likely autophosphorylation of Thr-286 allows the kinase to switch from a calmodulin-dependent to a calmodulin-independent state. CAMK2 is composed of four different chains: alpha, beta, gamma, and delta. The different isoforms assemble into homo- or heteromultimeric holoenzymes composed of 8 to 12 subunits. Expression of CAMK2 delta is significantly increased in patients suffering from dilated cardiomyopathy.
Rochlitz, H., et al., Diabetologia 43(4):465-473 (2000).
Hoch, B., et al., Circ. Res. 84(6):713-721 (1999).
Tombes, R.M., et al., Biochim. Biophys. Acta 1355(3):281-292 (1997).
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