Tumor Necrosis Factors (TNF) and Related Peptides

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Browse products name by alphabetical order:

CAT# Product Name M.W Molecular Formula Inquiry
R1723 TNF-α (10-36), human 2996.34 C131H211N43O38 Inquiry
R1724 TNF-α (46-65), human 2310.69 C110H172N24O30 Inquiry
T13001 CDIP2 2221.7 Inquiry
T13002 (Ile76)-TNF-α (70-80) (human) 1218.42 C55H91N15O16 Inquiry
T13003 P55 - TNFR Fragment 1342.5 Inquiry
T13004 P75 - TNFR Fragment 1204.4 Inquiry
T13005 Pro - TNF - α (71 - 82), human 1258.4 Inquiry
T13006 TNF - α (31 - 45), human 1667.9 Inquiry
T13007 TNF - α (72 - 82), human 1171.3 Inquiry
T13008 TRAF - binding Motif, acetylated, amide 611.7 Inquiry
T13009 Tumor Necrosis Factor Receptor, TNFR (159 - 178) Analog 2276.5 Inquiry
T13011 TNF-α (78-96) (human) 2101.44 C93H157N27O28 Inquiry


Tumor Necrosis Factor (TNF) is a kind of cytokine which can kill tumor cells directly without obvious toxicity to normal cells. All members of TNF family can express transmembrane proteins of type Ⅱ. It consists of three parts: the intracellular region of the amino terminal, the transmembrane region and the extracellular domain of the carboxyl terminal. TNF was mainly produced by activated macrophages, NK cells and T lymphocytes, which were divided into two types: TNF-α and TNF-β. The TNF produced by macrophages was named TNF-α, and the lymphotoxin (LT) produced by T lymphocytes was named TNF-β. The biological activity of TNF-α accounted for 70% ~ 95% of the total activity of TNF. Therefore, TNF usually refers to TNF-α. The precursor of human TNF-α consists of 233 amino acids, including a signal peptide composed of 76 amino acid residues.

Mechanism of action

Tumor necrosis factor receptor (TNFR) is the receptor of TNF-α. There are two subtypes of TNFR1 and TNFR2. TNFR exists on the surface of many normal cells and tumor cells, and TNF-α binds to target cells by TNFR. The cytolytic activity of TNFR1 cells plays a major role because of the death domain in the intracellular region of TNFR1. When the TNF-α trimer binds to the TNFR1 extracellular domain on the target cell membrane, PA DD binds to the TNFR1 death domain to form a TNFR1/IPA DD complex, which enlists a series of related proteins and triggers different downstream signaling pathways to achieve cytotoxicity. Antivirus, immune regulation and other biological functions.

Application of TNF

TNF-α plays an important role in many diseases, including rheumatoid arthritis, inflammatory bowel disease, septic shock, systemic lupus erythematosus (SLE), vasculitis and type I diabetes. Because of the complexity of the TNF-α related signaling pathway and its multiple roles in different diseases, although there is one-part of the proud success of the current treatment targeting TNF-α, there is still a lot of room for progress. Need constant exploration and improvement.


  1. Pan Yuchen, Wang Jiali, Hou Yayi. A. (2017). The research and development of TNF-α in autoimmune disease. 41(12):883-889.
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