GAPC2 Antibody

Glycolytic and Metabolic Roles

GAPC2 is a core enzyme in glycolysis, catalyzing the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. The antibody has been used to validate glycolytic activity in gapc1gapc2 double mutants, where reduced ATP/ADP ratios and NAD(P)H levels were observed . In overexpression (OE) lines, enhanced glycolytic flux and increased reducing power (NAD(P)H/NAD(P)) were confirmed via Western blotting .

Moonlighting Functions in Stress Responses

GAPC2 exhibits non-canonical roles in stress adaptation:

• Heat Stress: Overexpression of GAPC2 upregulates heat-inducible genes (HsfA2, DREB2C) .

• Pathogen Defense: gapc1gapc2 mutants show accelerated programmed cell death and increased ROS accumulation during bacterial infection .

• Viral Infection: GAPC2 interacts with viral components, modulating host-virus interactions .

Subcellular Localization and Protein Interactions

The antibody has been critical in mapping GAPC2’s localization and interactions:

1. Nuclear Localization: Co-immunoprecipitation (Co-IP) and bimolecular fluorescence complementation (BiFC) assays revealed GAPC2 interacts with NF-YC10, a nuclear transcription factor, during heat stress .

2. Vacuolar Trafficking: In germinating seeds, GAPC2 localizes to the prevacuolar compartment (PVC) via interaction with AtCAP2 (a syntaxin-like protein). Mutants lacking AtCAP2 show reduced membrane-associated GAPC2 and delayed lytic vacuole biogenesis .

Antibody Specificity

• Control Experiments: Western blotting confirmed the absence of GAPC2 signal in gapc2 knockout mutants, validating specificity .

• Cross-Reactivity: Predicted reactivity spans diverse plant species, including Brassica napus, Nicotiana tabacum, and Cucumis sativus .

Key Findings from Co-IP and Localization Studies