Pig CD64 Protein (In Vivo Grade, Ultra-Low Endotoxin) (ICH3020)

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This is recombinant pig (Sus scrofa domesticus) CD64 (FcgammaRI) protein, expressed in human embryonic kidney (HEK) 293 cells to preserve mammalian folding and glycosylation of the immunoglobulin-superfamily ectodomain. It corresponds to UniProt Q461Q0, the porcine high-affinity IgG Fc receptor. The protein is validated for binding and interaction studies including surface plasmon resonance (SPR), biolayer interferometry (BLI), and ELISA, where a correctly folded, glycosylated ectodomain is important for measuring IgG-Fc engagement. It is supplied as an in-vivo-grade, ultra-low-endotoxin preparation (<0.5 EU/mg), which suits demanding functional and cell-based work where endotoxin would otherwise confound Fc-receptor and myeloid-cell readouts. Available in bulk milligram-to-gram quantities for reproducible, lot-consistent use across assay development, antibody Fc-engineering campaigns, and species cross-reactivity screening. For research use only (RUO). As a recombinant receptor protein rather than an antibody, it carries no clone, isotype, or therapeutic dosing designation; content here is guidance for ichorbio to review before publishing. CD64 (FcgammaRI) is the only high-affinity Fc-gamma receptor, binding monomeric IgG with a dissociation constant near 10^-8 to 10^-9 M, whereas the other Fc-gamma receptors bind IgG only as immune complexes. Structurally it is distinguished by three extracellular C2-type immunoglobulin domains (EC1-EC3); the membrane-proximal EC2 and EC3 domains together mediate the high-affinity monomeric-IgG interaction. In pigs, FcgammaRI is a roughly 346-amino-acid transmembrane glycoprotein whose expression is conserved with other mammals. It is found chiefly on monocytes, macrophages, and dendritic cells, with inducible expression on neutrophils and eosinophils driven by IFN-gamma and G-CSF. Upon IgG engagement CD64 associates with the ITAM-bearing common FcR gamma chain to trigger activating signaling, driving phagocytosis, antibody-dependent cellular cytotoxicity, respiratory burst, and cytokine release. Porcine monomeric IgG binds the receptor with an affinity around 4x10^7 per molar.