|Other Names||Voltage-gated potassium channel subunit beta-3, K(+) channel subunit beta-3, Kv-beta-3, KCNAB3, KCNA3B|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5.|
|Tissue Location||Brain specific. Most prominent expression in cerebellum. Weaker signals detected in cortex, occipital lobe, frontal lobe and temporal lobe. Not detected in spinal cord, heart, lung, liver, kidney, pancreas, placenta and skeletal muscle.|
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Provided below are standard protocols that you may find useful for product applications.
Voltage-gated potassium (Kv) channels represent the mostcomplex class of voltage-gated ion channels from both functionaland structural standpoints. Their diverse functions includeregulating neurotransmitter release, heart rate, insulin secretion,neuronal excitability, epithelial electrolyte transport, smoothmuscle contraction, and cell volume. Four sequence-relatedpotassium channel genes - shaker, shaw, shab, and shal - have beenidentified in Drosophila, and each has been shown to have humanhomolog(s). This gene encodes a member of the potassium channel,voltage-gated, shaker-related subfamily. This member is one of thebeta subunits, which are auxiliary proteins associating withfunctional Kv-alpha subunits. This member and the KCNA5 geneproduct assemble into a heteromultimeric A-type channel thatinactivates completely and is significantly faster than otherA-type Kv channels.
Olsen, J.V., et al. Cell 127(3):635-648(2006)Olsen, J.V., et al. Cell 127(3):635-648(2006)Leicher, T., et al. J. Biol. Chem. 273(52):35095-35101(1998)McCormack, K., et al. FEBS Lett. 370 (1-2), 32-36 (1995) :
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