Visit our FAQ
Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888
Product Categories
Product Type
Application
Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

Explore how neutrophils shape the immune response in health and disease. This poster highlights neutrophil pathogen defense mechanisms, including phagocytosis, degranulation, and NETosis, as well as neutrophil roles in inflammation and NET-associated pathologies.
DOWNLOAD NOWTumor 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.1 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.1,2 Binding of TNF-α 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.3 Heterozygous mutations in TNFRSF1A are associated with tumor necrosis factor receptor-associated periodic syndrome (TRAPS), an autosomal dominant autoinflammatory syndrome.4 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 22.7 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.
WARNING This product is not for human or veterinary use.
1. Exploring TNFR1: From discovery to targeted therapy development. J. Transl. Med. 23(1), 71 (2025).
2. Selective inhibition of Tumor necrosis factor receptor-
3. TNF-
4. Revisiting TNF receptor-