• Product name
    Anti-TNFRSF1B antibody
  • Description
    Rabbit polyclonal to TNFRSF1B
  • Tested applications
    Suitable for: IHC-Pmore details
  • Species reactivity
    Reacts with: Human
    Predicted to work with: Mouse, Rat
  • Immunogen

    Synthetic peptide derived from the C terminal of Mouse TNFFRS1B.

  • Positive control
    • Human placenta tissue.



Our Abpromise guarantee covers the use of ab117543 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
IHC-P 1/50.


  • Relevance
    TNF RII (p75, CD120b) is a 75 kD transmembrane glycoprotein originally isolated from a human lung fibroblast library. Among the multitude of cells known to express TNFRII are monocytes, endothelial cells, Langerhans cells, and macrophages. Mouse to human amino acid sequence identity in the TNFRII cytoplasmic domain is 73 %, while amino acid sequence identity in the extracellular region falls to 58%. This drop in extracellular identity is reflected in the observation that human TNF-alpha is not active in the mouse system. TNF RII to TNF RI, amino acid sequence identity is only about 20% in the extracellular region and 5% in the cytoplasmic domain. TNF RII consists of a 240 amino acid residue extracellular region, a 27 amino acid residue transmembrane segment and a 173 amino acid residue cytoplasmic domain. TNF R1 and TNF R2 are members of a family of structurally related membrane receptors that includes lymphotoxin receptor, Fas, WSL1, DR4, CD40, CD30, CD27, 4-1BB, OX40, and p75 nerve growth factor receptor. Members of the TNFR family can interact through their cytoplasmic domains with a range of intracellular signalling proteins, most of which fall into two distinct groups. The first is the death domain containing proteins, including TRADD, FADD/MORT1, and RIP, which associate directly with receptors also containing death domains, such as TNF R1 and Fas. The second is the TRAF proteins. TRAF1 and TRAF2 were originally identified by their association with the cytoplasmic domain of TNFR2. TRAF proteins appear to function as adaptor proteins. TRAF2 directly binds at least eight intracellular molecules, including TRAF1, cIAP1, cIAP2, I-TRAF/TANK, A20, TRIP, RIP, and NIK. The best characterized TRAFmediated signal transduction pathway is the activation of NF-B transcription factors. TRAF2 mediates NF-B activation via the recruitment of the serine/threonine kinase NIK, which can in turn activate CHUK, an IBspecific kinase that triggers IB degradation. In addition to recruiting mediators of NF-B activation, TRAF2 can bind at least three other molecules (I-TRAF/TANK, A20, TRIP) that inhibit its ability to activate NF-B.
  • Cellular localization
    Plasma membrane and Secreted
  • Database links
  • Alternative names
    • CD120b antibody
    • Etanercept antibody
    • INN=Etanercept antibody
    • p75 antibody
    • p75 TNF receptor antibody
    • p75TNFR antibody
    • p80 TNF alpha receptor antibody
    • Soluble TNFR1B variant 1 antibody
    • TBPII antibody
    • TNF R II antibody
    • TNF R2 antibody
    • TNF R75 antibody
    • TNF RII antibody
    • TNFBR antibody
    • TNFR-II antibody
    • TNFR1B antibody
    • TNFR2 antibody
    • TNFR80 antibody
    • TNFRII antibody
    • Tumor necrosis factor beta receptor antibody
    • Tumor necrosis factor binding protein 2 antibody
    • Tumor necrosis factor receptor 2 antibody
    • Tumor necrosis factor receptor superfamily member 1B antibody
    • Tumor necrosis factor receptor type II antibody
    see all


  • ab117543 at 1/50 dilution staining TNFRSF1B in Formalin-fixed, Paraffin-embedded Human Placenta tissue by Immunohistochemistry.


This product has been referenced in:
  • Shivakumar P  et al. Preferential TNFa signaling via TNFR2 regulates epithelial injury and duct obstruction in experimental biliary atresia. JCI Insight 2:e88747 (2017). IF ; Mouse . Read more (PubMed: 28289704) »

See 1 Publication for this product

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