|Application ||WB, IP|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||95637 Da|
|Homology||Mouse - identical; human, rabbit - 15/17 amino acid residues identical.|
|Other Names||Potassium voltage-gated channel subfamily B member 1, Delayed rectifier potassium channel 1, DRK1, Voltage-gated potassium channel subunit Kv21, Kcnb1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (CY)HMLPGGGAHGSTRDQSI, corresponding to amino acid residues 841-857 of rat Kv2.1 (Accession P15387). Intracellular, C-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Application Details||Western blot analysis (WB): - Rat lung lysate (see Lv, Y. et al. (2013) in Product Citations). - Mouse heart lysate (see Huang, H. et al. (2013) in Product Citations). Immunoprecipitation (IP): - Xenopus oocyte membranes (see MacDonald, P.E. et al. (2002) in Product Citations). Immunohistochemistry (IH): - Human brain sections (1:500) (see Mezey, E. et al. (2003) in Product Citations). - Mouse pancreas sections (10 μg/ml) (see MacDonald, P.E. et al. (2002) in Product Citations). Immunocytochemistry (IC): - Mouse DRGs (see Bocksteins, E. et al. (2009) in Product Citations).|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||1 mg/ml.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
|Formulation||Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
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Provided below are standard protocols that you may find useful for product applications.
KV2.1 is a member of the voltage-gated K+ channel superfamily. Together with the closely related KV2.2 protein they form the KV2 subfamily also known as Shab.1 As with all KV channels, KV2.1 possesses the signature structure of the voltage-dependent K+ channels: six membrane-spanning domains with intracellular N and C termini. The functional KV channel is a tetramer that can either be a homotetramer or a heteromer of KV2.1 and KV2.2 subunits. Both KV2.1 and KV2.2 channels are known as delayed rectifiers that is, channels that are activated by changes in membrane potential (depolarization) but inactivate very slowly. The current they form is known as IK or IDR. Accessory subunits such as KChaP and the electrically silent a subunits KV8 and KV9 can modulate biochemical and biophysical properties of KV2.1.2 KV2.1 is widely expressed throughout the body including brain, lung, pancreas, skeletal muscle and pulmonary artery.2 The main function of KV2.1 is to maintain membrane potential and to modulate the electrical excitability in neurons and muscle. In rat pulmonary artery it probably mediates hypoxic pulmonary vasoconstriction together with the KV9.3 subunit.3 Several toxins from spider venoms are potent blockers (affecting the channels in the nanomolar range) of KV2.1channels. Among these the most potent and selective are Stromatoxin-1 (#STS-350), (12.7 nM)4 and Hanatoxin (42 nM).4
References 1. Albrecht, B. et al. (1993) Receptors Channels 1, 99. 2. Murakoshi, H. and Trimmer, J.S. (1999) J. Neurosci. 19, 1728. 3. Archer, S.L. et al. (1998) J. Clin. Invest. 101, 2319. 4. Escoubas, P. et al. (2002) Mol. Pharmacol. 62, 48.
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