Recombinant Rat TNF RI/TNFRSF1A Fc Chimera Protein, CF

Recombinant Rat TNF RI/TNFRSF1A Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: TNF RI/TNFRSF1A

TNF receptor 1 (TNF RI; also called TNF R‑p55/p60 and TNFRSF1A) is a 55 kDa type I transmembrane protein member of the TNF receptor superfamily, designated TNFRSF1A (1, 2). Rat TNF RI is a 461 amino acid (aa) protein that contains a 21 aa signal sequence, a 190 aa extracellular domain (ECD) with a PLAD (pre‑ligand assembly domain) that mediates constitutive dimer/trimer formation, followed by four CRD (cysteine-rich domains), a 23 aa transmembrane domain, and a 227 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain (3, 4). The ECD of rat TNF RI shares 69%, 88%, 66%, 68% and 75% aa sequence identity with human, mouse, canine, feline and porcine TNF RI, respectively. Both TNF RI and TNF RII (TNFRSF1B) are widely expressed and contain four TNF‑ alpha trimer-binding CRD in their ECD. However, TNF RI is thought to mediate most of the cellular effects of TNF‑ alpha (3). It is essential for proper development of lymph node germinal centers and Peyer’s patches, and for combating intracellular pathogens such as Listeria (1, 2, 5). TNF RI is also a receptor for TNF‑ beta /TNFSF1B (lymphotoxin‑ alpha ) (6). TNF RI is stored in the Golgi and translocates to the cell surface following pro‑inflammatory stimuli (7). TNF‑ alpha stabilizes TNF RI and induces its sequestering in lipid rafts, where it activates NF kappa B and is cleaved by ADAM-17/TACE (8  9, 16). Release of the 28‑34 kDa TNF RI ECD also occurs constitutively and in response to products of pathogens such as LPS, CpG DNA or S. aureus protein A (1, 10‑12). Full‑length TNF RI may also be released in exosome‑like vesicles (13). Release helps to resolve inflammatory reactions, since it down‑regulates cell surface TNF RI and provides soluble TNF RI to bind TNF‑ alpha (10, 14, 15). Exclusion from lipid rafts causes endocytosis of TNF RI complexes and induces apoptosis (1). Mutations of human TNF R1 can result in inflammatory episodes known as TRAPS (TNFR‑associated periodic syndrome) (7).

Related Research Areas

• Adipocytokines
• Cell Structure and Signaling Molecules
• Cytokine and Growth Factor Receptors on VSMC
• Cytokines and Receptors in Allergy and Asthma
• Cytokines and Receptors in Angiogenesis
• Diabetes
• Diabetic Peripheral Neuropathy
• EMT Induction
• Endothelial Cell Markers
• Obesity
• Platelet Cytokine and Growth Factor Receptors
• Regulation of Apoptosis by TNF Superfamily Members
• T Cell Cytokine Signaling
• TNF Superfamily Receptors