ATP6V1B2 Polyclonal Antibody, PerCP Conjugated

Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (AH) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.

ATP6B; ATP6V1 B; ATP6V1B; ATP6V1B; ATPase H+ transporting lysosomal 56/58kDa V1 subunit B; ; ATPase, H+ transporting, Endomembrane proton pump 58 kDa subunit; H+ transporting two sector ATPase; HO 57; HO57; V type proton ATPase subunit B, V-type proton ATPase subunit B; Vacuolar H+ ATPase 56,000 subunit; Vacuolar H+ ATPase 56000 subunit; Vacuolar proton pump subunit B