蛋白名称
Potassium voltage-gated channel subfamily B member 1
免疫原
The antiserum was produced against synthesized peptide derived from human Kv2.1. AA range:771-820
特异性
KV2.1 Polyclonal Antibody detects endogenous levels of KV2.1 protein.
组成
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
来源
Polyclonal, Rabbit,IgG
稀释比例
WB 1:500-2000;IHC-p 1:50-300; ELISA 2000-20000
纯化工艺
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
其他名称
KCNB1; Potassium voltage-gated channel subfamily B member 1; Delayed rectifier potassium channel 1; DRK1; h-DRK1; Voltage-gated potassium channel subunit Kv2.1
背景
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shab-related subfamily. This member is a delayed rectifier potassium channel and its activity is modulated by some other family members. [provided by RefSeq, Jul 2008],
功能
domain:The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.,domain:The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.,function:Mediates the voltage-dependent potassium ion permeability of excitable membranes. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient.,PTM:Highly phosphorylated on serine residues in the C-terminal. Differential phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-terminal Ser-15 are all regulated by calcineurin-mediated dephosphorylation. Particularly, Ser-
