Anti-ADH5/GSNOR Polyclonal Antibody for WB, IF/ICC, ELISA - P11766

Core Product Specifications and Parameters

Biological Background: ADH5/GSNOR Function and Localization

• ADH5 (alcohol dehydrogenase class-3) is a cytosolic enzyme also known as glutathione-dependent formaldehyde dehydrogenase (FALDH) and S-nitrosoglutathione reductase (GSNOR).
• Catalyzes the oxidation of long-chain primary alcohols and of S-(hydroxymethyl)glutathione. Related references: PMID:8460164
• Also oxidizes long-chain omega-hydroxy fatty acids like 20-HETE to dicarboxylic acids, impacting lipid signaling. Related references: PMID:16081420
• Essential for formaldehyde detoxification, preventing DNA damage. Related references: PMID:33355142
• Acts as an S-nitrosoglutathione reductase, modulating protein S-nitrosylation and nitric oxide signaling (by similarity).
• Localized in the cytoplasm; post-translational modifications include acetylation and phosphorylation; disease variants linked to dwarfism and intellectual disability (AMEDS/BMFS7).

Experimental Guidance and Technical Tips

• The immunogen spans the full-length human ADH5 protein (residues 1–374), suggesting broad epitope recognition. For WB, expect a band near 40 kDa and validate with appropriate positive controls (e.g., human, mouse, or rat tissue lysates).
• Cross-reactivity with mouse and rat is reported, allowing multi-species studies. Confirm band specificity in your model system.
• For IF/ICC, optimize fixation and permeabilization protocols to detect cytosolic ADH5.
• In ELISA, consider sandwich or indirect formats; pair with a matched monoclonal capture antibody if quantitative detection is needed.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio provides diagnostic manufacturers and research laboratories with a one-stop channel for high-quality IVD raw materials. In addition to this ADH5/GSNOR rabbit polyclonal antibody, we offer validated antibody pairs, optimized monoclonal/polyclonal antibodies, bulk ancillary reagents, and support for rare-target raw-material sourcing. Explore our portfolio to accelerate your oxidative stress and nitric oxide signaling research.