TNF RII/TNFRSF1B Protein, Human (235a.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 (235a.a, HEK293, mFc) is expressed by HEK293 and has a transmembrane region (M1-D257) 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].

Human

HEK293

C-mFc

P20333 (L23-D257)

7133  [NCBI]

65-75 kDa

Greater than 95% as determined by Tris-Bis PAGE.

<1 EU/μg, determined by LAL method.

• [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]