KCNAB1 Antibody(N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q14722 |
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Clone Names | 100623315 |
Gene ID | 7881 |
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Other Names | Voltage-gated potassium channel subunit beta-1, K(+) channel subunit beta-1, Kv-beta-1, KCNAB1, KCNA1B |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
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. |
Name | KCNAB1 |
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Synonyms | KCNA1B |
Function | Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:7499366, PubMed:7603988, PubMed:17156368, PubMed:17540341, PubMed:19713757). Modulates action potentials via its effect on the pore-forming alpha subunits (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members (PubMed:9763623). Promotes the closure of KCNA1, KCNA2 and KCNA5 channels (PubMed:7499366, PubMed:7890032, PubMed:7603988, PubMed:7649300, PubMed:8938711, PubMed:12077175, PubMed:12130714, PubMed:15361858, PubMed:17540341, PubMed:19713757). Accelerates KCNA4 channel closure (PubMed:7890032, PubMed:7649300, PubMed:7890764, PubMed:9763623). Accelerates the closure of heteromeric channels formed by KCNA1 and KCNA4 (PubMed:17156368). Accelerates the closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By similarity). Isoform KvB1.2 has no effect on KCNA1, KCNA2 or KCNB1 (PubMed:7890032, PubMed:7890764). Enhances KCNB1 and KCNB2 channel activity (By similarity). Binds NADPH; this is required for efficient down- regulation of potassium channel activity (PubMed:17540341). Has NADPH- dependent aldoketoreductase activity (By similarity). Oxidation of the bound NADPH strongly decreases N-type inactivation of potassium channel activity (By similarity). |
Cellular Location | Cytoplasm. Membrane {ECO:0000250|UniProtKB:P63144}; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note=Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits. |
Tissue Location | In brain, expression is most prominent in caudate nucleus, hippocampus and thalamus. Significant expression also detected in amygdala and subthalamic nucleus. Also expressed in both healthy and cardiomyopathic heart. Up to four times more abundant in left ventricle than left atrium. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Potassium channels represent the most complex class ofvoltage-gated ion channels from both functional and structuralstandpoints. Their diverse functions include regulatingneurotransmitter release, heart rate, insulin secretion, neuronalexcitability, epithelial electrolyte transport, smooth musclecontraction, and cell volume. Four sequence-related potassiumchannel genes - shaker, shaw, shab, and shal - have been identifiedin Drosophila, and each has been shown to have human homolog(s).This gene encodes a member of the potassium channel, voltage-gated,shaker-related subfamily. This member includes three distinctisoforms which are encoded by three alternatively splicedtranscript variants of this gene. These three isoforms are betasubunits, which form heteromultimeric complex with alpha subunitsand modulate the activity of the pore-forming alpha subunits.
References
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :Decher, N., et al. EMBO J. 27(23):3164-3174(2008)Cavalleri, G.L., et al. Lancet Neurol 6(11):970-980(2007)Lamesch, P., et al. Genomics 89(3):307-315(2007)Lunetta, K.L., et al. BMC Med. Genet. 8 SUPPL 1, S13 (2007) :
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