Anti-XPO6 Rabbit Polyclonal Antibody for WB and ELISA - Q96QU8

Core Product Specifications and Parameters

Biological Background: XPO6 Function and Localization

• Exportin-6 (XPO6), also named Ran-binding protein 20 (RANBP20), functions as a nuclear transport receptor mediating nuclear export.
• It specifically exports actin and profilin-actin complexes from the nucleus in somatic cells, linking nuclear transport to cytoskeletal organization.
• The protein dynamically localizes to both the nucleus and cytoplasm, consistent with its role in nucleocytoplasmic shuttling.
• Post-translational modifications, including acetylation and phosphorylation, may regulate its transport activity and protein interactions.
• Alternative splicing produces multiple isoforms, potentially diversifying its functional repertoire.
• XPO6 is part of the proteomics identification and reference proteome projects, underscoring its broad biological significance.

Experimental Guidance and Technical Tips

• The immunogen targets a region within amino acids 116–216 of human XPO6, which shares high homology with mouse, supporting the observed cross-reactivity.
• For Western blot, anticipate a band near 127–128 kDa; run reducing SDS-PAGE and validate signal in relevant human or mouse cell lysates.
• ELISA applications may require antibody titration to determine the optimal working concentration for your assay format.
• Confirm specificity by including appropriate positive and negative controls, and consider knockout or siRNA validation in your sample system.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio is your integrated partner for IVD raw-material sourcing, offering antibodies, validated pairs, and ancillary reagents to accelerate diagnostic development. This XPO6 antibody supports research into nucleocytoplasmic transport and actin dynamics, and we can complement it with bulk monoclonal/polyclonal antibodies, rare-target reagents, and tailored sourcing solutions. Let CamelBio streamline your supply chain from discovery to clinical application.