The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Constituents: 10% Trehalose, 1% Human serum albumin, PBS
This product is an active protein and may elicit a biological response in vivo, handle with caution.
It is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial.
p75 TNF receptor
p80 TNF alpha receptor
p80 TNF-alpha receptor
Soluble TNFR1B variant 1
TNF R II
Tumor necrosis factor beta receptor
Tumor necrosis factor receptor 2
Tumor necrosis factor receptor superfamily member 1B
Tumor necrosis factor receptor type II
Tumor necrosis factor-binding protein 2
Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity.
Contains 4 TNFR-Cys repeats.
Phosphorylated; mainly on serine residues and with a very low level on threonine residues. A soluble form (tumor necrosis factor binding protein 2) is produced from the membrane form by proteolytic processing.
Recombinant human TNF Receptor II protein (Fc Chimera) 图像
Functional Studies - TNF Receptor II protein (Fc Chimera Active) (ab83541)
Post-translational modifications result in protein heterogeneity. The densitometry scan demonstrates that ab83541 exists in multiple isoforms, which differ according to their level of post-translational modification. Expression of these isoforms is highly significant for cell biology, as they more closely resemble the native human proteins. The triangle indicates theoretical pI and MW of the protein.
Recombinant human TNF Receptor II protein (Fc Chimera) (ab83541)参考文献
has not yet been referenced specifically in any publications.