Anti-GUCY1A3 Polyclonal Antibody for WB, IF/ICC, ELISA - Q02108

Core Product Specifications and Parameters

Biological Background: GUCY1A3 Function and Localization

• GUCY1A3 encodes the soluble guanylate cyclase subunit alpha-1 (also known as alpha-3, GCS-alpha-3), which dimerizes with a beta subunit to form the active heterodimeric enzyme responsible for converting GTP to cGMP.
• The protein contains nucleotide-binding (GTP) and catalytic lyase domains critical for cGMP biosynthesis.
• Alternative splicing generates multiple isoforms, expanding functional diversity.
• The protein localizes predominantly to the cytoplasm.
• Tissue-specific expression has been confirmed at the protein level in brain cortex and lung.
• It is identified as a phosphoprotein and catalogued as a reference proteome entry with proteomics identification support.

Experimental Guidance and Technical Tips

• The immunogen corresponds to the N‑terminal region (aa 1–120) of human GUCY1A3; consider this when selecting peptide blocking or epitope mapping experiments.
• For Western blot (WB), a band near 77 kDa is expected; validate in relevant human, mouse, or rat tissue/cell lysates.
• In immunofluorescence/immunocytochemistry (IF/ICC), anticipate cytoplasmic staining; include appropriate fixation and permeabilization controls.
• ELISA applications may require checkerboard titration to determine optimal coating antigen and antibody concentrations.
• As a polyclonal antibody, assess lot‑to‑lot consistency and consider pre‑adsorption steps if non‑specific bands appear.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio provides diagnostic manufacturers and research institutions with streamlined access to verified IVD raw materials, technical services, and consulting—from concept to clinic. This anti‑GUCY1A3 polyclonal antibody supports soluble guanylate cyclase studies, and we offer complementary sourcing for validated antibody pairs, recombinant proteins, bulk ancillary reagents, and rare‑target raw materials to accelerate your assay development.