GAPDH Specific Neutra™ Antibody Products

Are prolonged drug development timelines or inconsistent antibody validation impeding your breakthroughs? Creative Biolabs' anti-GAPDH Neutra™ antibodies leverage high-fidelity hybridoma screening and advanced epitope mapping to ensure precise neutralization of GAPDH, accelerating your research in metabolic disorders, neurodegenerative diseases, and viral pathogenesis.

Introduction to GAPDH

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme central to glycolysis, catalyzing the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate. Ubiquitously expressed across prokaryotes and eukaryotes, GAPDH exhibits exceptional evolutionary conservation, with over 76% sequence homology between species. While traditionally recognized as a housekeeping protein, emerging studies underscore its roles in non-metabolic processes, including apoptosis, DNA repair, and vesicular trafficking.

• Structure

GAPDH functions as a homotetramer, with each subunit (~36 kDa) comprising an NAD+-binding domain and a catalytic domain. The quaternary structure enables cooperative binding of substrates and regulatory ligands. Structural studies reveal that post-translational modifications—such as S-nitrosylation or acetylation—induce conformational shifts, modulating its enzymatic and non-canonical activities.

• Related Signaling Pathways

Beyond glycolysis, GAPDH interfaces with key pathways:

- Apoptosis: Nuclear translocation of GAPDH under oxidative stress activates p53-mediated cell death.

- Autophagy: GAPDH binds to Rab2A, regulating autophagosome-lysosome fusion.

- Immune Response: During viral infections, GAPDH interacts with viral RNA, influencing replication and host immune evasion.

Fig.1 The non-glycolytic roles of GAPDH.¹

• Pathologies Associated with GAPDH Dysregulation

Aberrant GAPDH expression or activity is implicated in diverse pathologies. In cancer, elevated GAPDH drives glycolytic flux to support tumor proliferation. Neurodegenerative disorders like Alzheimer's disease correlate with oxidative stress-induced GAPDH aggregation, while viral pathogens (e.g., hepatitis, influenza) exploit GAPDH for replication. Additionally, hyperglycemia in diabetes enhances GAPDH S-nitrosylation, contributing to endothelial dysfunction.

Fig.2 The mechanisms of GAPDH aggregation.¹

Applications of Anti-GAPDH Neutralizing Antibodies

• Mechanistic Studies in Disease Pathogenesis

Anti-GAPDH antibodies enable precise dissection of GAPDH's dual roles in metabolism and disease. For example, neutralizing antibodies can block GAPDH-mediated glycolysis in cancer cells, sensitizing them to chemotherapy. In neurodegeneration research, these antibodies help detect pathological aggregates in post-mortem brain tissues.

• Diagnostic Biomarker Development

GAPDH overexpression in tumors or its presence in extracellular vesicles serves as a biomarker for early cancer detection. Neutralizing antibodies enhance diagnostic specificity by differentiating between intact GAPDH and proteolytic fragments in liquid biopsies.

• Antiviral Therapeutic Strategies

Certain viruses hijack GAPDH to stabilize their RNA or evade immune recognition. Neutralizing antibodies targeting GAPDH-viral protein complexes reduce viral load in preclinical models, offering a novel antiviral mechanism.

• Therapeutic Targeting in Metabolic Disorders

In diabetic complications, GAPDH inhibitors derived from neutralizing antibodies mitigate oxidative damage in vascular tissues. These antibodies also aid in screening small-molecule inhibitors that disrupt GAPDH's interaction with pro-inflammatory mediators.

Our Anti-GAPDH Neutralizing Antibodies

Creative Biolabs' anti-GAPDH antibodies are rigorously validated for specificity and functional blocking. Key features include:

- High Affinity: Engineered to target conserved regions (e.g., catalytic Cys152), ensuring cross-reactivity across human, murine, and primate models.

- Functional Neutralization: Effectively inhibits enzymatic activity and disrupts interactions with viral proteins or apoptotic mediators.

- Versatile Validation: Optimized for applications such as immunoblotting (detection ~36 kDa band), immunofluorescence (subcellular localization), and ELISA (quantify serum GAPDH in metabolic syndromes).

Creative Biolabs offers anti-GAPDH Neutra™ antibodies, empowering researchers to unravel the complexities of this multifunctional enzyme and translate findings into therapeutic innovations.

Contact our team today to discuss custom solutions for your projects, from antibody validation to co-development partnerships.

REFERENCE

1. Butera, Giovanna, et al. "Regulation of autophagy by nuclear GAPDH and its aggregates in cancer and neurodegenerative disorders." International Journal of Molecular Sciences 20.9 (2019): 2062. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/ijms20092062