ATP6V1F Protein, Human (GST)

ATP6V1F is an important subunit of the vacuolar (H+)-ATPase (V-ATPase) V1 complex and is an important component of this enzyme's role in cellular pH regulation. It forms a catalytic AB heterodimer and peripheral stem that plays a role in ATP hydrolysis. ATP6V1F Protein, Human (GST) is the recombinant human-derived ATP6V1F protein, expressed by E. coli , with N-GST labeled tag. The total length of ATP6V1F Protein, Human (GST) is 119 a.a., with molecular weight of ~40 KDa.

ATP6V1F, a vital subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), constitutes part of the multisubunit enzyme that plays a central role in cellular pH regulation. This enzyme is a heteromultimeric assembly comprising two essential complexes: the ATP-hydrolytic V1 complex and the proton translocation V0 complex. Within the V1 complex, ATP6V1F contributes to the formation of the catalytic AB heterodimers, constituting a heterohexamer, and the peripheral stalks comprised of EG heterodimers. Additionally, it is an integral part of the central rotor, working in concert with subunit D. The V1 complex is responsible for ATP hydrolysis, whereas the V0 complex, in which ATP6V1F is not directly mentioned but is implied, is crucial for proton translocation across membranes. This proton transport involves various subunits, including the proton transport subunit a, a ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f, and accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR. The cooperative action of these subunits underscores the significance of ATP6V1F in the intricate machinery of V-ATPase, which acidifies and maintains pH in cellular compartments and, in certain cell types, at the plasma membrane, thereby influencing various physiological processes.

Human

E. coli

N-GST

Q16864 (M1-R119)

9296  [NCBI]

Approximately 40 kDa.

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.