Recombinant Human TNF RI/TNFRSF1A Fc Avi-tag Protein, CF Summary
|Human TNF RI/TNFRSF1A|
Accession # P19438.1
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Biotinylated Recombinant Human TNF RI/TNFRSF1A Fc Chimera Avi-tag Protein (Catalog # AVI10910) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 54-65 kDa and 108-130 kDa, respectively.
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). Human TNF RI is a 455 amino acid (aa) protein that contains a 21 aa signal sequence and 190 aa 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 221 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain (3, 4). The ECD of human TNF RI shows 70%, 69%, 80%, 80%, and 73% aa identity with mouse, rat, canine, feline and porcine TNF RI, respectively; and it shows 23% aa identity with the ECD of TNF RII. 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). Our Avi-tag Biotinylated human TNFRI/TNFRSF1A Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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