K + Channel alpha (AA 995-1113) antibody

Details for Product No. ABIN968436, Supplier: Log in to see
AA 995-1113
Human, Mouse (Murine), Rat (Rattus)
Clonality (Clone)
Monoclonal ()
Immunofluorescence (IF), Western Blotting (WB)
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Immunogen Human K+ Channel alpha Subunit aa. 995-1113
Clone 32-K Channel
Isotype IgG1
Cross-Reactivity Rat (Rattus), Mouse (Murine)
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 The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Background 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 alpha subunit (hslo) and the regulatory beta subunit. The alpha subunit is subject to direct phosphorylation by cyclic GMP-dependent protein kinase (PKG) and dephosphorylation by protein phosphatase 2A. The fact that the alpha 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.
Molecular Weight 125 kDa

Related Products: ABIN968545, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 μg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Store undiluted at -20°C.
Supplier Images
Western Blotting (WB) image for anti-K + Channel alpha (AA 995-1113) antibody (ABIN968436) Western blot analysis of K+ Channel alpha on rat brain lysate. Lane 1: 1:250, lane 2:...
Product cited in: Alioua, Tanaka, Wallner, Hofmann, Ruth, Meera, Toro: "The large conductance, voltage-dependent, and calcium-sensitive K+ channel, Hslo, is a target of cGMP-dependent protein kinase phosphorylation in vivo." in: The Journal of biological chemistry, Vol. 273, Issue 49, pp. 32950-6, 1999 (PubMed).

Díaz, Meera, Amigo, Stefani, Alvarez, Toro, Latorre: "Role of the S4 segment in a voltage-dependent calcium-sensitive potassium (hSlo) channel." in: The Journal of biological chemistry, Vol. 273, Issue 49, pp. 32430-6, 1999 (PubMed).

Stefani, Ottolia, Noceti, Olcese, Wallner, Latorre, Toro: "Voltage-controlled gating in a large conductance Ca2+-sensitive K+channel (hslo)." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 10, pp. 5427-31, 1997 (PubMed).

Meera, Wallner, Jiang, Toro: "A calcium switch for the functional coupling between alpha (hslo) and beta subunits (KV,Ca beta) of maxi K channels." in: FEBS letters, Vol. 382, Issue 1-2, pp. 84-8, 1996 (PubMed).

Background publications Wallner, Meera, Toro: "Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N terminus." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, Issue 25, pp. 14922-7, 1997 (PubMed).