Product Name: CAM Kinase 2 alpha Antibody
Species Reactivity: Dog, Human, Mouse, Orangutan, Rat
Tested Applications: ELISA, IF, IHC, WB
Applications: CAM Kinase 2 alpha antibody can be used in Western Blot starting at 5 – 10 μg/mL, immunohistochemistry starting at 5 μg/mL, and immunoprecipitation.
User Note: Optimal dilutions for each application to be determined by the researcher.
Predicted Molecular Weight:
Immunogen: CAM Kinase 2 alpha antibody was raised against amino acids 6-23 of CAM Kinase 2 alpha (Human).
Host Species: Rabbit
Purification: Purified
Physical State: Liquid
CAS NO.: 890643-16-0
Product: DC_05
Buffer: 0.02 M potassium phosphate, 0.15 M sodium chloride, pH 7.2, 0.01% sodium azide.
Concentration:
Storage Conditions: Store CAM Kinase 2 alpha antibody at -20 ˚C prior to opening. Dilute only prior to immediate use. For extended storage aliquot contents and freeze at -20 ˚C or below. As with all antibodies avoid freeze/thaw cycles.
Clonality: Polyclonal
Conjugate: Unconjugated
Alternate Names: CAMK2A, AlphaCaMKII, CaM-kinase II alpha chain, CaMK-II subunit alpha, CAMKA, CaM kinase II alpha, CaMK II alpha, CaMK-II alpha subunit, CaMKIINalpha, CaM kinase II alpha subunit, CaM kinase II subunit alpha, CaMKII alpha, CaMKIIalpha, KIAA0968
Accession NO.: Q9UQM7
Protein Ino: 296434552
Official Symbol: CAMK2A
Geneid: 815
Background: CaM Kinase II (also known as CAMK2 and calcium/calmodulin-dependent protein kinase type II alpha chain) is a prominent kinase in the central nervous system that may function in the long-term potentiation of neurotransmitter release. CaM Kinase II autophosphorylates itself at Thr-286 which allows the kinase to switch from a calmodulin-dependent to a calmodulin-independent state. CaM Kinase II 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. This kinase is expressed in brain tissue. Alternative splicing occurs for this gene product.
PubMed ID:http://aac.asm.org/content/43/2/264.abstract
