An E.coli-derived zebrafish Atp6v1a recombinant protein (amino acids A37-D617) was used as the immunogen for the Zebrafish Atp6v1a antibody.
ATP6V1A encodes the catalytic A subunit of the V1 domain of the vacuolar-type H+-ATPase (V-ATPase), a multi-subunit enzyme complex responsible for acidifying intracellular compartments in eukaryotic cells. The V-ATPase plays a crucial role in diverse cellular processes, including protein degradation, receptor-mediated endocytosis, and neurotransmitter loading into synaptic vesicles.The Atp6v1a protein forms the core of the V1 domain, where it contributes to ATP hydrolysis, driving proton translocation across membranes via the V0 domain. This acidification is essential for maintaining cellular homeostasis, lysosomal function, and pH-dependent signaling pathways.In zebrafish (Danio rerio), Atp6v1a is highly conserved and broadly expressed during development, particularly in neural, renal, and gastrointestinal tissues. It serves as a model for studying V-ATPase function in vertebrate development, organogenesis, and disease models such as neurodegeneration and cancer.
