TNF-β (human, recombinant)

TNF-β, also known as lymphotoxin-α (LT-α), is a cytokine and member of the TNF and TNF receptor (TNFR) cytokine superfamily.¹ It is produced as an N-glycosylated peptide that forms soluble bell-shaped homotrimers after signal peptide cleavage.^2,3 TNF-β also forms cell surface-anchored heterotrimers with TNF-C, also known as lymphotoxin-β (LT-β).³ It is expressed in T cells, natural killer (NK) cells, and B cells, as well as macrophages. When secreted, TNF-β homotrimers bind to TNF-α receptor 1 (TNFR1) and TNFR2 while TNF-β-LT-β heterotrimers bind to the LT-β receptor.^1,4,2 Through activation of these receptors, TNF-β is involved in lymphoid organ development and maintenance, host defense, and inflammatory processes.^3,1 TNF-β induces proliferation of fibroblast-like synoviocytes isolated from patients with rheumatoid arthritis, and levels of TNF-β are increased in the serum and synovial fluid of patients with rheumatoid arthritis.⁵ SNPs in LTA, the gene encoding TNF-β in humans, are associated with various diseases, including systemic lupus erythematosus (SLE) and cancer.^6,7 Cayman’s TNF-β (human, recombinant) protein can be used for cellular activity assays. The protein was synthesized from a DNA sequence encoding the mature form of human TNF-β (Leu35-Leu205) with an N-terminal translation-initiating methionine (Met1). The expressed protein consists of 172 amino acids, has a calculated molecular weight of 18.8 kDa, and a predicted N-terminus of Met1.

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