Anti-SMUG1 Polyclonal Antibody for WB and ELISA - Q53HV7

Core Product Specifications and Parameters

Biological Background: SMUG1 Function and Localization

• SMUG1 (Single-strand selective monofunctional uracil DNA glycosylase) is a DNA repair enzyme that initiates base excision repair by recognizing and removing damaged or misincorporated uracil from DNA.
• It preferentially acts on single-stranded DNA substrates but also processes double-stranded DNA, with highest activity toward U/G mismatches and uracil derivatives (5-formyluracil, 5-hydroxyuracil, 5-hydroxymethyluracil).
• The enzyme is specific for uracil and its oxidized derivatives; it does not excise analogous cytosine derivatives or other oxidized bases, and its activity is damage-specific and salt-dependent.
• Encoded by the SMUG1 gene, alternative splicing generates multiple isoforms.
• Subcellularly localized to the nucleus, consistent with its role in genomic DNA repair.
• Classified as a hydrolase and DNA-binding protein, involved in DNA damage and DNA repair pathways.

Experimental Guidance and Technical Tips

• For Western blot (WB), consider using a starting dilution range of 1:500 to 1:2000 and validate detection in the appropriate species and tissue lysates.
• For ELISA, test serial dilutions of antibody to optimize the signal-to-noise ratio against the immunogen or target protein.
• Since the immunogen is the full-length recombinant human SMUG1 protein, the antibody may recognize both native and denatured forms of the target; verify performance under your specific assay conditions.
• Cross-reactivity is reported for human and mouse; confirm reactivity with other species if needed.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio provides diagnostic manufacturers and research labs with one-stop access to validated IVD raw materials, including this SMUG1 polyclonal antibody for DNA repair research. From antigen-specific polyclonal antibodies and bulk ancillary reagents to custom sourcing of rare targets, we support every stage of assay development.