GAPC1 Antibody
Description
Understanding GAPC1 Antibody
GAPC1 antibody is a specific immunological reagent targeting the cytosolic glyceraldehyde-3-phosphate dehydrogenase (GAPDH) enzyme in Arabidopsis thaliana. GAPC1 (AT3G04120) is a key enzyme in glycolysis, catalyzing the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. It exists as two isoforms (GAPC1 and GAPC2), sharing 98% amino acid identity . The antibody is critical for studying its role in metabolic regulation, stress responses, and cellular localization.
Detection and Quantification of GAPC1
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Western Blot:
Protein Interaction Studies
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Co-Immunoprecipitation:
Subcellular Localization
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Fluorescence Microscopy:
Research Findings and Functional Insights
Critical Observations
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Moonlighting Functions: GAPC1’s role extends beyond glycolysis, including transcriptional regulation and stress responses .
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Isoform Specificity: Antibodies must distinguish GAPC1 from GAPC2 due to their high sequence similarity (98% identity) .
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Cross-Reactivity: While not explicitly tested, monoclonal antibodies like mAb5B7 (targeting bacterial GapC) highlight conserved epitopes across species .
Product Specs
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
GAPC1 Antibody is a key enzyme involved in glycolysis, catalyzing the conversion of D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate, initiating the glycolytic pathway. Its role is critical in maintaining cellular ATP levels and regulating carbohydrate metabolism. GAPC1 is essential for full fertility and plays a vital role in the plant's response to oxidative stress. It mediates plant responses to abscisic acid (ABA) and water deficits, activating PLDDELTA and producing phosphatidic acid (PA), a key signaling lipid in plant stress responses.
GAPC1 associates with FBA6 to the outer mitochondrial membrane, in a redox-dependent manner, leading to actin binding and bundling. This process occurs under oxidizing conditions and is reversible under reducing conditions. GAPC1 may be part of a redox-dependent retrograde signaling network, facilitating adaptation to oxidative stress. It also demonstrates the ability to bind DNA in vitro.
- The redox-dependent localization of GapC1 and GapC2 in various cellular compartments, along with their interactions with VDAC3 and Trx-h3, have been studied (PMID: 30189844).
- The E3 ubiquitin-ligase SEVEN IN ABSENTIA like 7 mono-ubiquitinates GAPC1 in vitro, a crucial process for its nuclear localization (PMID: 26582368).
- Upon perception of bacterial flagellin, GAPC1 exhibits dynamic responses, including a significant increase in fluorescent puncta size and enhanced nuclear accumulation (PMID: 25918875).
- FERONIA, a key protein in plant development, controls leaf starch accumulation through interaction with GAPC1 (PMID: 26232644).
- GAPC levels are critical for overall cellular production of reductants, energy, and carbohydrate metabolites, demonstrating a direct correlation with seed oil accumulation (PMID: 24989043).
- GAPC1's high sensitivity to the cellular redox state suggests its role in oxidative stress signaling or protection in plants (PMID: 23569110).
- The H(2)O(2)-promoted interaction of GAPC and PLDdelta provides a direct link between membrane lipid-based signaling, energy metabolism, and growth control in the plant response to reactive oxygen species (ROS) and water stress (PMID: 22589465).
- The addition of GSSG, and more effectively, S-nitrosoglutathione, has been shown to inactivate the enzymes GapC1 and GapC2 from various organisms, including Arabidopsis thaliana, spinach, yeast, and rabbit muscle (PMID: 18298409).
