Mouse Monoclonal VMA2 antibody. Suitable for WB, ICC/IF and reacts with Saccharomyces cerevisiae samples. Cited in 2 publications.
pH: 7.5
Preservative: 0.02% Sodium azide
Constituents: HEPES buffered saline
WB | ICC/IF | |
---|---|---|
Saccharomyces cerevisiae | Tested | Expected |
Species | Dilution info | Notes |
---|---|---|
Species Saccharomyces cerevisiae | Dilution info 0.25-1 µg/mL | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Saccharomyces cerevisiae | Dilution info 20 µg/mL | Notes - |
Non-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 (PubMed:2141385). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (PubMed:2141385).
VMA2
VAT2, YBR127C, YBR1002, VMA2, V-type proton ATPase subunit B, V-ATPase subunit B, V-ATPase 57 kDa subunit, Vacuolar proton pump subunit B
Mouse Monoclonal VMA2 antibody. Suitable for WB, ICC/IF and reacts with Saccharomyces cerevisiae samples. Cited in 2 publications.
pH: 7.5
Preservative: 0.02% Sodium azide
Constituents: HEPES buffered saline
Near homogeneity as judged by SDS-PAGE (purity >95%). The antibody was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation.
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VMA2 also known as V-type proton ATPase subunit B enzyme plays a role in the assembly and function of the V-ATPase complex that acidifies cellular compartments. This protein has a mass of approximately 57 kDa. VMA2 localizes to membrane structures and is expressed highly in yeast and other eukaryotic organisms. Its main role is maintaining the proton gradient across the vacuolar membrane influencing several cellular processes.
VMA2 functions as part of the V-ATPase complex which is essential for cellular energy regulation and the acidification of vacuoles and endosomes. This complex contributes to cellular homeostasis by facilitating pH regulation and ion transport. VMA2 as a non-catalytic subunit assists with the stabilization of the enzyme structure and participates in proton transport processes that impact numerous cellular activities.
VMA2 influences protein sorting and vesicle trafficking within the endocytic and secretory pathways. It collaborates with proteins like VMA9 and VMA13 to regulate these processes. The function of the V-ATPase complex including VMA2 integrates into pathways like the pH signaling pathway and vesicular trafficking ensuring proper cellular functions like nutrient uptake and protein degradation.
VMA2 has been linked to conditions like osteopetrosis and Fanconi syndrome. These disorders relate to improper acidification due to dysfunctional V-ATPase. VMA2's association with VMA4 and other V-ATPase components becomes important in understanding the molecular basis of these diseases shedding light on possible therapeutic targets or disease markers.
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All lanes: Western blot - Anti-VMA2 antibody [13D11B2] (ab113684)
All lanes: Yeast whole cell lysate at 15 µg
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 58 kDa
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