Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Sodium azide is a reversible inhibitor of oxidative metabolism; therefore, antibody preparations containing this preservative agent must not be used in cell cultures nor injected into animals. Sodium azide may be removed by washing stained cells or plate-bound antibody or dialyzing soluble antibody in sodium azide-free buffer. Since endotoxin may also affect the results of functional studies, we recommend the NA/LE (No Azide/Low Endotoxin) antibody format, if available, for in vitro and in vivo use.
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- Species cross-reactivity detected in product development may not have been confirmed on every format and/or application.
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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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