TNF RII/TNFRSF1B Protein, Human (183a.a, HEK293, mFc)

TNFRII (TNFRSF1B) protein has a high ability to bind with tumor necrosis factor-alpha (TNF-α). TNFRII has pro-apoptotic function. TNFRII recruits TRAF2, induces gene expression and intensively crosstalks with TNF-R1. TNFRII selectively enhances the induction of apoptosis by the death receptor TNFRI. TNF RII/TNFRSF1B Protein, Human (183a.a, HEK293, mFc) is expressed by HEK293 and has a transmembrane region (P24-T206) with mFc tag at the C-terminus^[1].

TNFRII (TNFRSF1B) protein is a single-pass type I membrane protein belonging to the tumor necrosis factor (TNF) family. TNFRII is the major signaling receptor for TNF-α. TNFRII protein is highly regulated and typically found in immune system cells^[1].
The amino acid sequence of mouse TNFRII protein has low homology between human and rhesus macaque TNFRII protein (less than 85%). The amino acid sequence of TNFRII protein in human and rhesus macaque is very similar (percent identity matrix of 95.88%).
TNFRII induces apoptosis. TNFRII does not directly engage the apoptotic program, but relies on the induction of endogenous, membrane-bound TNF, which subsequently activates TNFRI. TNFRII stimulates the action of the endogenously produced membrane-bound TNF on TNFRI is drastically enhanced. TNFRII competes with TNFRI for the recruitment of newly synthesized TRAF2-bound anti-apoptotic factors, thereby promoting the formation of a caspase-8-activating TNFRI complex. TNFRII competes with TNFRI for binding of TRAF2 and the TRAF2-associated anti-apoptotic cIAP1 and cIAP2 proteins. cIAP1-initiated degradation of TRAF2, which in turn enhances receptor competition for the remaining TRAF2, cIAP1 and cIAP2 molecules. cIAP1 would have an anti-apoptotic function upon recruitment into the TNFRI signalling complex, but would switch to a net proapoptotic function upon recruitment into the TNFRII signalling complex^[1][2][3].

Measured by its ability to inhibit the TNF-alpha mediated cytotoxicity in the L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED₅₀ for this effect, in the presence of 0.25 ng/mL of TNF-alpha, is 0.004302 µg/mL, corresponding to a specific activity is 2.325×10⁵ U/mg.

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  Measured by its ability to inhibit the TNF-alpha mediated cytotoxicity in the L-929 mouse fibroblast cells in the presence of the metabolic inhibitor actinomycin D. The ED₅₀ for this effect, in the presence of 0.25 ng/mL of TNF-alpha, is 0.004302 µg/mL. corresponding to a specific activity is 2.325×10⁵ U/mg.

Human

HEK293

C-mFc

P20333-1 (P24-T206)

7133  [NCBI]

Partial

PAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWVPECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPT

Approximately 60 kDa, based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

<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.

• [1]. Wajant H, et, al. Tumor necrosis factor signaling. Cell Death Differ. 2003 Jan;10(1):45-65.  [Content Brief]

  [2]. Fotin-Mleczek M, et, al. Apoptotic crosstalk of TNF receptors: TNF-R2-induces depletion of TRAF2 and IAP proteins and accelerates TNF-R1-dependent activation of caspase-8. J Cell Sci. 2002 Jul 1;115(Pt 13):2757-70.  [Content Brief]

  [3]. Masli S, et, al. Anti-inflammatory effects of tumour necrosis factor (TNF)-alpha are mediated via TNF-R2 (p75) in tolerogenic transforming growth factor-beta-treated antigen-presenting cells. Immunology. 2009 May;127(1):62-72.  [Content Brief]