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Western blot analysis of K+ Channel α on rat brain lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-K+ Channel α.


BD Transduction Laboratories™ Purified Mouse Anti K+ Channel α

Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml .
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
Cellular excitability is modulated by the precise function of voltage-sensitive ion channels. Large conductance potassium channels (Maxi-K) are unique in that they are sensitive to transmembrane potential and intracellular Ca2+ concentrations. These channels, important for neuronal firing and vascular tone, share many features with voltage-dependent Na+, Ca2+, and K+ channels. Among these are the S4 region, a motif with a repeated triple sequence of one positively charged amino acid and two hydrophobic amino acids. This region is thought to be the voltage sensor. Maxi-K is subject to complex metabolic control control that also involves G proteins and phosphorylation/dephosphorylation reactions. This type of K+ channel is composed of two subunits, the pore-forming α subunit (hslo) and the regulatory β subunit. The α subunit is subject to direct phosphorylation by cyclic GMP-dependent protein kinase (PKG) and dephosphorylation by protein phosphatase 2A. The fact that the α subunit of Maxi-K channels is a substrate of PKG supports the idea that these channels perform an important function in the cellular response to potent vasodilators, such as nitrocompounds and atrial natiuretic peptide.
Development References (4)
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Alioua A, Tanaka Y, Wallner M, et al. The large conductance, voltage-dependent, and calcium-sensitive K+ channel, Hslo, is a target of cGMP-dependent protein kinase phosphorylation in vivo. J Biol Chem. 1998; 273(49):32950-32956. (Biology). View Reference
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Diaz L, Meera P, Amigo J, et al. Role of the S4 segment in a voltage-dependent calcium-sensitive potassium (hSlo) channel. J Biol Chem. 1998; 273(49):32430-32436. (Biology). View Reference
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Meera P, Wallner M, Jiang Z, Toro L. A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels. FEBS Lett. 1996; 382(1-2):84-88. (Biology). View Reference
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Stefani E, Ottolia M, Noceti F, et al. Voltage-controlled gating in a large conductance Ca2+-sensitive K+channel (hslo). Proc Natl Acad Sci U S A. 1997; 94(10):5427-5431. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
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