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Western blot analysis of CaM Kinase II expression on a rat cerebrum lysate (left panel). Rat Cerebrum Lysate (Cat. No. 611463) was stained with Purified Mouse Anti-CaM Kinase II (Cat. No. 611292/611293) at dilutions of 1: 1:2500, 1:5000, and 1:10,000 (lanes 1, 2, and 3 respectively). CaM Kinase II expression was visualized with HRP Goat Anti-Mouse Ig (Cat. No. 554002) and appears as a 52 kDa band. Immunohistochemical analysis of CaM Kinase II expression on rat brain (center panel). Formalin-fixed paraffin-embedded section without citrate buffer pretreatment (10X magnification). Immunofluorescence analysis of CaM Kinase II expression on SK-N-SH cells (Human neuroblastoma; ATCC HTB-11) (right panel). Cells were seeded in a collagen coated 384-well imaging plate at ~ 8,000 cells per well. After overnight incubation, cells were stained using the methanol fix/perm protocol and Purified Mouse Anti-CaM Kinase II. The second step reagent used was Alexa Fluor® 488 goat anti-mouse Ig (Invitrogen) (pseudo colored green). Cell nuclei were counter stained with Hoechst 33342 (pseudo colored blue). Images was taken either on a BD Pathway™ 855 or 435 Bioimager System with a 20x objective and merged using BD AttoVision™ software. This antibody also stains SH-SY5Y, C6, U87 and U373 cells using both the Triton X-100 and methanol fix/perm protocols.
BD Transduction Laboratories™ Purified Mouse Anti-CaM Kinase II
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- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
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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, α and β, at a ratio of 2:1 and homomers of α 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 α and β subunits, which results in a substantial increase in its affinity for Ca2+/calmodulin.
Development References (5)
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Brocke L, Chiang LW, Wagner PD, Schulman H. Functional implications of the subunit composition of neuronal CaM kinase II. J Biol Chem. 1999; 274(32):22713-22722. (Biology). View Reference
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Fallon L, Moreau F, Croft BG, Labib N, Gu WJ, Fon EA. Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain. J Biol Chem. 2002; 277(1):486-491. (Biology: Western blot). View Reference
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Hanson PI, Schulman H. Neuronal Ca2+/calmodulin-dependent protein kinases. Annu Rev Biochem. 1992; 61:559-601. (Biology). View Reference
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Ishida A, Fujisawa H. Stabilization of calmodulin-dependent protein kinase II through the autoinhibitory domain. J Biol Chem. 1995; 270(5):2163-2170. (Biology). View Reference
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Zong H, Ren JM, Young LH, et al. AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. Proc Natl Acad Sci U S A. 2002; 99(25):15983-15987. (Biology: Western blot). View Reference
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