Active • Host: HEK293 cells • AA: 22-211 • Tag: C-terminal His • MW: 22.7 kDa
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TNFRSF1A/CD120a Extracellular Domain (human, recombinant)

Item No. 44198

Product Insert (PDF)
Technical Information
Synonyms
  • CD120a
  • TNFR1
  • TNF-R1
  • TNFR-I
  • Tumor Necrosis Factor Receptor 1
  • Tumor Necrosis Factor Receptor Superfamily Member 1A
Purity
≥92% estimated by SDS-PAGE
Endotoxin Testing
<1.0 EU per μg of the protein as determined by the LAL method
Source
Active recombinant human C-terminal His-tagged TNFRSF1A extracellular domain expressed in HEK293 cells
Amino Acids
22-211
MW
22.7 kDa
Lyophilized from sterile PBS, pH 7.4
UniProt Accession №
P19438
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    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.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.

    References & Product Citations
    Product Description References

    1. Li, Y., Ye, R., Lin, J., et alExploring TNFR1: From discovery to targeted therapy development. J. Transl. Med. 23(1), 71 (2025).

    2. Zhang, N., Wang, Z., and Zhao, Y. Selective inhibition of Tumor necrosis factor receptor-1 (TNFR1) for the treatment of autoimmune diseases. Cytokine Growth Factor Rev. 55, 80-85 (2020).

    3. Ferreira França, F.B., Silva, M.V., Silva, M.F., et alTNF-TNFR1 signaling enhances the protection against Neospora caninum infection. Front Cell. Infect. Microbiol. 11, 789398 (2022).

    4. Cudrici, C., Deuitch, N., and Aksentijevich, I. Revisiting TNF receptor-associated periodic syndrome (TRAPS): Current perspectives. Int. J. Mol. Sci. 21(9), 3263 (2020).