Anti-Zebrafish Atp6v1a

0.5mg/ml if reconstituted with 0.2ml sterile DI water. 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. Protein function: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. May play a role in neurite development and synaptic connectivity. [The UniProt Consortium]