*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
human peripheral blood lymphocytes
The antibody detects human TNF sRII and shows no cross-reactivity with recombinant human TNF sRI.
PBS, 5% trehalose
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
recombinant human TNF soluble receptor II (TNF sRII) expressed in Escherichia coli. The immunogen is the non-glycosylated, N-terminal methionyl form of the naturally-occurring human soluble type II receptor for TNF, minus 53 amino acids from the proline-rich region just exterior to the transmembrane domain.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Tnf Receptor Superfamily Member 1B,Cd120B,Tbpii,Tnf-R-Ii,Tnf-R75,Tnfbr,Tnfr1B,Tnfr2,Tnfr80,P75,P75Tnfr,Tnfrsf1B
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, 41BB, 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, c-IAP1, c-IAP2, I-TRAF/TANK, A20, TRIP, RIP, and NIK (Hsu et al). 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.