Anti-RNASE3 Rabbit Polyclonal Antibody for IHC-P and ELISA - P12724

Core Product Specifications and Parameters

Biological Background: RNASE3 Function and Localization

• RNASE3 (eosinophil cationic protein, ECP) is a secreted effector of eosinophils with low-efficiency ribonuclease activity and potent cytotoxicity against helminths and bacteria.
• It disrupts bacterial membranes by promoting depolarization and outer membrane detachment, exhibiting broad antimicrobial activity against both Gram-negative and Gram-positive strains.
• The protein belongs to the pancreatic ribonuclease A superfamily and plays a critical role in innate host defense and inflammatory responses.
• Subcellular localization is primarily extracellular following secretion from activated eosinophils.
• RNASE3 is a glycoprotein featuring multiple intramolecular disulfide bonds, and its 3D structure has been solved, highlighting key residues for function.
• Post-translational modifications such as nitration can occur, potentially modulating biological activity.

Experimental Guidance and Technical Tips

• The immunogen (amino acids 28–160) corresponds to the mature, secreted form of RNASE3, enabling detection of the processed protein free of the signal peptide.
• For immunohistochemical staining (IHC-P), optimize antigen retrieval steps and validate the antibody on eosinophil-containing tissue sections known to express ECP.
• In ELISA, the polyclonal format may capture diverse epitopes; perform serial dilution experiments to determine the optimal working concentration for your particular assay setup.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio offers diagnostic developers and research institutes a single access point for premier IVD raw materials. This anti-RNASE3 antibody supports investigations into innate immunity and inflammatory disorders. Complementing our catalog, CamelBio supplies validated antibody pairs, bulk ancillary reagents, and bespoke sourcing for challenging targets to drive your assay from concept to clinical application.