TNF alpha/TNFSF2 protein, Human (His)
Based on 8 publication(s) in Google Scholar
Tumour Necrosis Factor alpha (TNF alpha) is a potent pro-inflammatory cytokine. TNF alpha binds to its receptors, mainly TNFR1 and TNFR2, and then transmits molecular signals for biological functions such as inflammation and cell death. TNF alpha stimulates NF-κB pathway via TNFR2 promotes cancer growth, invasion, and metastasis. Anti-TNF-α MAb significantly suppresses the tumor development in colitis-associated cancer (CAC) mouse. TNF alpha as a proneurogenic factor activates the SAPK/JNK Pathway and can facilitate neuronal replacement and brain repair in response to brain injury. TNF alpha/TNFSF2 protein, Human (His) is a recombinant protein with a N-Terminal His label, It consists of 157 amino acids (V77-L233) and is produced in CHO cells.
- Species: Human
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- References
- Help & FAQs
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Biological Activity
Tumour Necrosis Factor alpha (TNF alpha) is a potent pro-inflammatory cytokine[1]. TNF alpha binds to its receptors, mainly TNFR1 and TNFR2, and then transmits molecular signals for biological functions such as inflammation and cell death[2]. TNF alpha stimulates NF-κB pathway via TNFR2 promotes cancer growth, invasion, and metastasis. Anti-TNF-α MAb significantly suppresses the tumor development in colitis-associated cancer (CAC) mouse[3]. TNF alpha as a proneurogenic factor activates the SAPK/JNK Pathway and can facilitate neuronal replacement and brain repair in response to brain injury[4]. TNF alpha/TNFSF2 protein, Human (His) is a recombinant protein with a N-Terminal His label, It consists of 157 amino acids (V77-L233) and is produced in CHO cells.
TNF alpha is produced by various types of cells including macrophages, monocytes, neutrophils, T cells, and NK-cells[2].
The amino acid sequence of human TNF alpha protein has low homology between mouse, rat, bovine, cynomolgus TNF alpha protein. While, human TNF alpha shares 94.85% aa sequence identity with cynomolgus TNF alpha protein, mouse TNF alpha shares 94.47% aa sequence identity with rat TNF alpha protein.
TNF alpha exists in two forms; a type II transmembrane protein (tmTNF-α) and a mature soluble protein (sTNF-α). TNF-α binds to its receptors, mainly TNFR1 and TNFR2, and then transmits molecular signals for biological functions such as inflammation and cell death. Both sTNF-α and tmTNF-α activate TNFR1, and process a death domain (DD) that interacts with the TNFR1-associated death domain (TRADD) adaptor protein. The TNFR2 signaling pathway is mainly activated by tmTNF-α. TNFR1 signaling tends to be pro-inflammatory and apoptotic. TNFR2 results in NF-κB and MAPKs and AKT activation, TNFR2 activation is associated with homeostatic bioactivities such as tissue regeneration, cell proliferation, and cell survival, as well as host defense and inflammation[1].
TNF-alpha is critical for normal immune response, abnormal secretion TNF alpha activates synovial fibroblasts, keratinocytes, osteoclasts, induces rheumatoid arthritis, inflammatory bowel disease, psoriatic arthritis (PsA), and noninfectious uveitis (NIU)[3]. TNF alpha positively regulates endogenous TNF-α expression levels independently of Pgp efflux activity, induces IHF cells proliferation[4]. TNF alpha in tissues may promote cancer growth, invasion, and metastasis. Besides, TNF alpha stimulates NF-κB pathway via TNFR2 and anti-TNF-α MAb significantly suppresses the tumor development in colitis-associated cancer (CAC) mouse[5]. TNF alpha as a proneurogenic factor activates the SAPK/JNK pathway and can facilitate neuronal replacement and brain repair in response to brain injury[6].
TNF alpha (human) (0, 10, 15, 20, 30, 50 ng/mL; 24, 48 h) reduces KB-C1 cells viability at 30 ng/mL after 48 h, reduces pro-caspase-3, cleaved caspase-3 expression in KB-C1 and KB-3-1 cells[4].
TNF alpha (human) (10, 15 ng/mL; 24 h) significantly increases the mRNA levels of Pgp (ABCB1) in KB-3-1 cells, and promotes expressive reduction on total Pgp protein levels and a slightly decreases in cell surface-Pgp in KB-C1 cells, and stimulates IHF cells proliferation, probably via ERK activation[4].
TNF alpha (human) (100 µg; osmium pump in back; daily for 7 days) significantly increases in the number of inflammatory cells and the degree of synovial inflammation is significantly exacerbated in twenty-four SCID-HuRAg mice[7].
1. Measured in a cytotoxicity assay using L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is < 0.13 ng/mL.
2. Loaded Brivekimig (HY-P990907) on AHC2 biosensor, can bind TNF alpha protein, Human (His) with an affinity constant of <1.0E-12 M as determined in BLI assay.
Publications (8)
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Journal Impact Factor
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Most Recent
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Adv Sci (Weinh)
ETV4 Promotes Colorectal Cancer Progression by Reprogramming Asparagine Metabolism to Remodel the Stromal Microenvironment. [Abstract]2026 Mar 20:e16557. PMID: 41861091 -
Sci Adv
Deficient chaperone-mediated autophagy facilitates LPS-induced microglial activation via regulation of the p300/NF-κB/NLRP3 pathway. [Abstract]2023 Oct 6;9(40):eadi8343. PMID: 37801503
TNF alpha/TNFSF2 protein, Human (His) purchased from MedChemExpress. Usage Cited in: Sci Adv. 2023 Oct 6;9(40):eadi8343. [Abstract]
U2OS cells were treated with TNF-α (20 ng/ml) for 24 hours. The protein levels of p300 and LAMP2A were measured using immunoblot analyses.
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Med
Real-time diagnosis of cholangiocarcinoma by combining digestive endoscopy and optic fiber biosensors based on bile clusterin. [Abstract]2025 Sep 2:100843. PMID: 40930098 -
J Immunother Cancer
HSP47 inhibition-induced CD155 expression through TRAF2 deubiquitination promotes tumor immune evasion. [Abstract]2025 Nov 28;13(11):e011976. PMID: 41314980
TNF alpha/TNFSF2 protein, Human (His) purchased from MedChemExpress. Usage Cited in: J Immunother Cancer. 2025 Nov 28;13(11):e011976. [Abstract]
Western blot analysis of CD155 expression in OS cells treated with exogenous TNF-α, showing concentration- and time-dependent upregulation. TNF-α at increasing concentrations (0, 10, 20, 30 ng/mL for 24 hours) and varying time points (0, 6, 12, 24 hours at 10 ng/mL) upregulates CD155 in U2OS and K7M2 cells. GAPDH serves as a loading control.
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Int J Mol Med
Selective autophagic degradation of glycolytic activator PFKFB3 contributes to maintaining intestinal epithelial barrier in inflammatory bowel disease. [Abstract]2026 Feb;57(2):43. PMID: 41384306
TNF alpha/TNFSF2 protein, Human (His) purchased from MedChemExpress. Usage Cited in: Int J Mol Med. 2026 Feb;57(2):43. [Abstract]
Autophagic flux was measured by transfecting cells with mRFP-GFP-LC3 dual-fluorescence adenovirus (Ad-LC3), allowing differentiation between autophagosomes (mRFP+/GFP+ fluorescence, appearing as yellow puncta) and autolysosomes (mRFP+/GFP-fluorescence, appearing as red puncta). TNF-α (200 ng/ml) induced epithelial cells for 48 h. Representative immunofluorescence images were shown. (Original magnification, ×20). Quantification of LC3 puncta number of representative cells.
TNF alpha/TNFSF2 protein, Human (His) purchased from MedChemExpress. Usage Cited in: Int J Mol Med. 2026 Feb;57(2):43. [Abstract]
Relative glucose content and lactate (Lac) production in control vs. TNF-α (200 ng/ml, 24 h) induced epithelial cells.
TNF alpha/TNFSF2 protein, Human (His) purchased from MedChemExpress. Usage Cited in: Int J Mol Med. 2026 Feb;57(2):43. [Abstract]
BCECF fluorescent counter-staining in TNF-α (200 ng/ml, 24 h) induced epithelial cells vs. control. Representative immunofluorescence images were shown.
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Free Radic Biol Med
METTL14/m6A/CEBPD axis: A critical player in chronic cerebral hypoperfusion-associated neuroinflammation. [Abstract]2026 Jun:249:89-102. PMID: 41791683 -
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Technical Parameters
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Species Human
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Source E. coli
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Tag N-6*His
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Accession
P01375 (V77-L233)
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Molecular Construction
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N-term
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6*His
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TNF alpha (V77-L233)
Accession # P01375 -
C-term
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Protein Length
Full Length of TNF soluble form
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Synonyms
TNF; Tumor Necrosis Factor (TNF Superfamily, Member 2); Prev. TNFA; Tumor Necrosis Factor-Alpha; TNF-Alpha; Tumor Necrotic Factor Alpha; TNFSF2; TNF Superfamily, Member 2; Tumor Necrosis Factor Ligand Superfamily Member 2; TNF, Macrophage-Derived; TNF-A;
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AA Sequence
VRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELRDNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRETPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL
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Predicted Molecular Mass
17.4 kDa
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Molecular Weight
Approximately 18 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 90%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder
1.Lyophilized from a 0.22 μm filtered solution of PBS, 300 mM NaCl, pH 7.4.
2.Lyophilized from a 0.22 μm filtered solution of PBS.
3.Lyophilized from a 0.22 μm filtered solution of PBS, pH 6.5, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (265 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
[1]. Horiuchi T, et al. Transmembrane TNF-alpha: structure, function and interaction with anti-TNF agents. Rheumatology (Oxford). 2010 Jul;49(7):1215-28. [Content Brief]
[2]. El-Tahan RR, et al. TNF-α gene polymorphisms and expression. Springerplus. 2016 Sep 7;5(1):1508. [Content Brief]
[3]. Jang DI, et al. The Role of Tumor Necrosis Factor Alpha (TNF-α) in Autoimmune Disease and Current TNF-α Inhibitors in Therapeutics. Int J Mol Sci. 2021 Mar 8;22(5):2719. [Content Brief]
[4]. Berguetti T, et al. TNF-α Modulates P-Glycoprotein Expression and Contributes to Cellular Proliferation via Extracellular Vesicles. Cells. 2019 May 24;8(5):500. [Content Brief]
[5]. Onizawa M, et al. Signaling pathway via TNF-alpha/NF-kappaB in intestinal epithelial cells may be directly involved in colitis-associated carcinogenesis. Am J Physiol Gastrointest Liver Physiol. 2009 Apr;296(4):G850-9. [Content Brief]
[6]. Bernardino L, et al. Tumor necrosis factor-alpha modulates survival, proliferation, and neuronal differentiation in neonatal subventricular zone cell cultures. Stem Cells. 2008 Sep;26(9):2361-71. [Content Brief]
[7]. Matsuno H, et al. The role of TNF-alpha in the pathogenesis of inflammation and joint destruction in rheumatoid arthritis (RA): a study using a human RA/SCID mouse chimera. Rheumatology (Oxford). 2002 Mar;41(3):329-37. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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