Customize vha-13 Antibody

Description

Molecular Identity of vha-13

vha-13 (gene: Y49A3A.2) encodes subunit A of the cytosolic V1 domain of V-ATPase. This enzyme hydrolyzes ATP to transport protons across membranes, regulating lysosomal pH and cellular processes like protein degradation and ion balance . Key features include:

Domain Structure: V1 domain (ATP hydrolysis) and V0 domain (proton translocation) .
Functional Partners: Forms a heterohexamer with VHA-12 to drive V-ATPase rotor activity .
Regulation: Expression is modulated by calcineurin and miR-1, impacting muscle function and longevity .

Antibody-Based Detection in Research

Studies employ transgenic C. elegans strains expressing tagged vha-13 fusion proteins. Antibodies against these tags enable precise tracking:

Tag	Antibody Used	Application	Key Findings
3xFlag::mNeonGreen	Anti-Flag/GFP antibodies	Localization in muscle, hypodermis, and gut	VHA-13 localizes to dense bodies (Z-disks) in muscle and lysosomal compartments .
His-tagged	Anti-His antibody (sc-8036)	Vesicle profiling in hypodermal cells	VHA-13 co-localizes with VHA-5 and VHA-8 on apical vesicles critical for multivesicular body (MVB) biogenesis .

3.1. Muscle Homeostasis and Lysosomal Regulation

miR-1 Interaction: miR-1 represses vha-13 via two binding sites in its 3′UTR. Mutation of these sites de-represses VHA-13 expression, exacerbating motility defects in mir-1 mutants .
Localization: In body wall muscle, VHA-13 is enriched at dense bodies and cytosol, supporting ATPase activity for lysosomal acidification .

3.2. Role in Multivesicular Body (MVB) Biogenesis

Vesicle Dynamics: RNAi of vha-13 disrupts VHA-5::RFP and VHA-8::GFP vesicle patterns, reducing MVB density. This highlights VHA-13’s role in coordinating V-ATPase assembly for vesicle acidification .
Genetic Interactions: vha-13 knockdown phenocopies fln-2 mutants, linking V-ATPase activity with filamin-mediated MVB formation .

Regulatory Mechanisms and Disease Relevance

Calcineurin Dependence: VHA-13 levels are inversely correlated with calcineurin activity, suggesting cross-talk between calcium signaling and lysosomal function .
Longevity Pathways: Reduced VHA-13 activity improves mid-life motility and extends lifespan in mir-1-overexpressing strains, implicating lysosomal pH in aging .

Technical Challenges and Future Directions

Antibody Limitations: Existing tools detect epitope-tagged VHA-13 but lack specificity for endogenous protein. Development of direct antibodies would enhance functional studies.
Therapeutic Potential: Modulating V-ATPase activity via vha-13 could address lysosomal storage disorders or muscle degenerative diseases .

Product Specs

Buffer

Preservative: 0.03% ProClin 300; Constituents: 50% Glycerol, 0.01M PBS, pH 7.4

Form

Liquid

Lead Time

14-16 weeks (Made-to-order)

Synonyms

vha-13 antibody; Y49A3A.2 antibody; V-type proton ATPase catalytic subunit A antibody; V-ATPase subunit A antibody; EC 7.1.2.2 antibody; V-ATPase 69 kDa subunit antibody; Vacuolar H ATPase protein 13 antibody; Vacuolar proton pump subunit alpha antibody

Target Names

vha-13

Uniprot No.

Q9XW92

Target Background

Function

The vha-13 antibody targets the catalytic subunit of the peripheral V1 complex within the vacuolar ATPase (V-ATPase). V-ATPase is crucial for acidifying various intracellular compartments in eukaryotic cells. Specifically, vha-13 plays a vital role in the removal of protein aggregates that accumulate in immature oocytes within the distal gonad. This aggregate clearance is triggered by sperm introduction during mating, occurring prior to fertilization and only after the oocytes mature and migrate to the proximal gonad. Sperm introduction initiates V-ATPase accumulation in proximal oocytes, leading to lysosomal acidification. This acidification facilitates the engulfment and subsequent clearance of protein aggregates by lysosomes. Furthermore, lysosomal acidification alters mitochondrial morphology and function. In immature distal oocytes, mitochondria exhibit fragmentation, elevated reactive oxygen species (ROS) production, and high membrane potential, signifying metabolic inactivity. Conversely, in mature proximal oocytes, mitochondria transition to a tubular morphology with reduced ROS levels and membrane potential, indicative of a metabolically active state essential for aggregate mobilization and subsequent clearance.

Database Links

KEGG: cel:CELE_Y49A3A.2

STRING: 6239.Y49A3A.2.4

UniGene: Cel.38650

Protein Families

ATPase alpha/beta chains family

Tissue Specificity

Expressed in proximal but not distal germ cells.

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vha-13 Antibody