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Details for Product No. ABIN968457

Calcium/calmodulin-Dependent Protein Kinase II alpha (CAMK2A) (AA 448-460) antibody

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Antigen
Synonyms CAMKA, PKCCD, PK2CDD, zgc:112538, zgc:123320, camk2, camk2b
Epitope
»Alternatives AA 448-460
Reactivity
»Alternatives Rat (Rattus)
Host
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
Application
»Alternatives Western Blotting (WB), BioImaging (BI), Immunofluorescence (IF), Immunohistochemistry (IHC)
Pubmed 5 references available
Catalog no. ABIN968457
Quantity 50 µg
Price
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Immunogen Rat CaM Kinase IIalpha
Clone DF7
Isotype IgG1
Cross-Reactivity Mouse (Murine), Human, Dog (Canine)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Purity Purified
Alternative Name CaM Kinase II
Background Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) is a multifunctional Ser/Thr kinase that regulates a number of cellular functions in response to increased intracellular Ca2+. CaM kinase II is widely distributed, but is predominantly expressed in brain. It is involved in the regulation of neuronal functions such as neurotransmitter synthesis, neurotransmitter release, long-term potentiation, and formation of spatial learning. Neuronal CaM kinase II contains heteromers of two major subunits, alpha and beta, at a ratio of 2:1 and homomers of alpha subunits. Each subunit has N-terminal ATP-binding and catalytic/regulatory domains and a C-terminal association domain. The regulatory domain consists of the autoinhibitory and calmodulin-binding sites. Assembly of the association domains of multiple subunits positions the regulatory domains for intersubunit autophosphorylation. After binding Ca2+/calmodulin, CaM kinase II undergoes rapid autophosphorylation of the alpha and beta subunits, which results in a substantial increase in its affinity for Ca2+/calmodulin.
Synonyms: Ca2+/calmodulin-dependent protein kinase II
Molecular Weight 52 kDa
Research Area Kinases/Phosphatases
Comment

Related Products: ABIN967389, ABIN968545

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Storage -20 °C
Product cited in: Hanson, Schulman: "Neuronal Ca2+/calmodulin-dependent protein kinases." in: Annual review of biochemistry, Vol. 61, pp. 559-601, 1992 (PubMed).

Ishida, Fujisawa: "Stabilization of calmodulin-dependent protein kinase II through the autoinhibitory domain." in: The Journal of biological chemistry, Vol. 270, Issue 5, pp. 2163-70, 1995 (PubMed).

Brocke, Chiang, Wagner et al.: "Functional implications of the subunit composition of neuronal CaM kinase II." in: The Journal of biological chemistry, Vol. 274, Issue 32, pp. 22713-22, 1999 (PubMed).

Fallon, Moreau, Croft et al.: "Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain." in: The Journal of biological chemistry, Vol. 277, Issue 1, pp. 486-91, 2002 (PubMed).

Zong, Ren, Young et al.: "AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 25, pp. 15983-7, 2002 (PubMed).

Alternatives for antigen "Calcium/calmodulin-Dependent Protein Kinase II alpha (CAMK2A)", type "Antibodies"
Hosts (69), (33), (7)
Reactivities (73), (61), (43), (10), (7), (7), (6), (6), (5), (5), (3), (2), (2), (1), (1), (1), (1)
Applications (103), (43), (27), (26), (14), (13), (8), (8), (3), (3), (3), (2), (2), (2), (1)
Epitopes (25), (12), (7), (6), (4), (4), (3), (3), (3), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
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