Anti-K_Vβ1 Antibody

Voltage-gated K⁺ channels represent a structurally and functionally diverse group of membrane proteins. These channels establish the resting membrane potential and modulate the frequency and duration of action potentials in nerve and muscle¹. The duration of the open states of K⁺ channels is determined by the rates of deactivation and inactivation. K_V channels are hetero-oligomeric complexes consisting of two different types of subunits: membrane-bound, pore-forming α subunits and the smaller β subunits. The β subunits appear to be peripheral proteins tightly associated with the cytoplasmic side of the α subunits². 

The inactivation gate can be formed by an N-terminal segment of an auxiliary β-subunit, as in the complex of K_Vβ1 and K_Vα family channels³. There are three mammalian K_Vβ genes: K_Vβ1, K_Vβ2 and K_Vβ3. Additional variability in the K_Vβ1 family results from alternative splicing in the amino terminal region, thus yielding the K_Vβ1.1, K_Vβ1.2, and K_Vβ1.3 subunits⁴.