4-1BB / TNFRSF9 Recombinant Protein Cat. No.: 11-324

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psi-iconSpecifications
SPECIES:Rabbit
SOURCE SPECIES:HEK293 cells
SEQUENCE:Val 29 - Ile 191
FUSION TAG:His Tag
TESTED APPLICATIONS:ELISA, WB
APPLICATIONS:This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 18.8 kDa. The protein migrates as 27-33 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
psi-iconProperties
PURITY:>90% as determined by SDS-PAGE.
PREDICTED MOLECULAR WEIGHT:18.8 kDa
PHYSICAL STATE:Lyophilized
BUFFER:PBS, pH7.4
STORAGE CONDITIONS:Lyophilized Protein should be stored at -20˚C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20˚C or -70˚C. Avoid repeated freeze-thaw cycles.
psi-iconAdditional Info
ALTERNATE NAMES:TNFRSF9,4-1BB,CD137,CDw137,ILA
ACCESSION NO.:XP_008264195.1
OFFICIAL SYMBOL:TNFRSF9
GENE ID:100348914
psi-iconBackground and References
BACKGROUND:4-1BB is also known as CD137, tumor necrosis factor receptor superfamily member 9 (TNFRSF9), induced by lymphocyte activation (ILA), is a co-stimulatory molecule of the tumor necrosis factor (TNF) receptor superfamily. CD137 can be expressed by activated T cells, but to a larger extent on CD8 than on CD4 T cells. In addition, CD137 expression is found on dendritic cells, follicular dendritic cells, natural killer cells, granulocytes and cells of blood vessel walls at sites of inflammation. The best characterized activity of CD137 is its costimulatory activity for activated T cells. Crosslinking of CD137 enhances T cell proliferation, IL-2 secretion survival and cytolytic activity. Further, it can enhance immune activity to eliminate tumors in mice. CD137 can enhance activation-induced T cell apoptosis when triggered by engagement of the TCR/CD3 complex. In addition, 4-1BB/4-1BBL co-stimulatory pathway has been shown to augment secondary CTL responses to several viruses, and meanwhile augment anti-tumor immunity. 4-1BB thus is a promising candidate for immunotherapy of human cancer. CD137 has been shown to interact with TRAF2.
REFERENCES:1) Cooper D, et al., 2002, Eur. J. Immunol. 32 (2): 521–9.
2) Jang, I K., et al., 1998, Biochem. Biophys. Res. Commun. (UNITED STATES) 242 (3): 613–20.
3) Arch, R H., Thompson C B., 1998, Mol. Cell. Biol. (UNITED STATES) 18 (1): 558–65.

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