TNFRSF1A/CD120a Extracellular Domain (human, recombinant)

Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A), also known as CD120a and tumor necrosis factor receptor 1 (TNFR1), is a transmembrane receptor with roles in inflammatory immune responses. It is composed of an extracellular domain that contains four cysteine-rich domains (CRD1-4), a transmembrane domain, and an intracellular domain comprising a neutral sphingomyelinase domain, a TNFR1 internalization domain, and an AIP-binding domain, all of which have roles in signal complex assembly. TNFRSF1A is ubiquitously expressed and localized to the plasma membrane. Binding of TNF-alpha to TNFRSF1A induces receptor activation and induction of pro-apoptotic and pro-inflammatory signaling pathways. Tnfrsf1a-/- increases mortality and parasite burden and reduces serum levels of IgG1 in a mouse model of N. caninum infection. Heterozygous mutations in TNFRSF1A are associated with tumor necrosis factor receptor-associated periodic syndrome (TRAPS), an autosomal dominant autoinflammatory syndrome. Cayman's TNFRSF1A/CD120a Extracellular Domain (human, recombinant) protein can be used for binding assay and Western blot (WB) applications. This protein consists of 201 amino acids, has a calculated molecular weight of 22. kDa, and a predicted N-terminus of Ile22 after signal peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 30-35 kDa due to glycosylation.