Anti-PAG1 Monoclonal Antibody for WB, ELISA - Q9NWQ8

Core Product Specifications and Parameters

Biological Background: PAG1/Cbp Function and Localization

• PAG1 (also known as Csk-binding protein, Cbp, or transmembrane adapter protein PAG) is a ubiquitously expressed transmembrane phosphoprotein.
• It localizes to the cell membrane, specifically in lipid rafts, serving as an adapter for signal transduction.
• In T-cells, PAG1 negatively regulates TCR-mediated signaling by recruiting CSK to lipid rafts, leading to LCK inhibition and dampening T-cell activation.
• Similarly, in mast cells, it negatively regulates FCER1-mediated signaling.
• PAG1 inhibits immunological synapse formation by preventing dynamic arrangement of lipid raft proteins.
• It may also play a role in cell adhesion signaling.
• As a phosphoprotein, its function is modulated by phosphorylation, and it is palmitoylated for membrane raft targeting.
• It is a key component in adaptive immunity, with expression in immune cells including T-cells, B-cells, and monocytes.

Experimental Guidance and Technical Tips

• The immunogen corresponds to a C-terminal sequence (aa 333-432); in WB, expect a band near 47 kDa in lysates from immune cells (e.g., Jurkat, spleen). Validate in your relevant species.
• For ELISA, this antibody can be used to detect recombinant or endogenous PAG1; optimize coating and detection conditions for your specific matrix.
• To confirm cross-reactivity in mouse and rat, consider aligning the immunogen sequence with the orthologous proteins.
• Store as recommended (e.g., -20°C) after shipment on ice bags to preserve stability.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio serves as a comprehensive one-stop partner for IVD raw materials, offering this anti-PAG1 clone to support immunology and oncology assay development. Beyond individual antibodies, we supply validated antibody pairs, optimized monoclonals, bulk ancillary reagents, and custom sourcing for rare targets, enabling seamless transition from concept to clinical application.