Recombinant Cynomolgus Monkey PVRIG Fc Chimera Protein, CF Summary
|Cynomolgus Monkey PVRIG|
(Gly20, Ser21 or Glu23-Leu172)
Accession # XP_005549281.1
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.
When Recombinant Cynomolgus Monkey PVRIG Fc Chimera (Catalog # 10718-CV) is immobilized at 1.00 µg/mL (100 µL/well), Recombinant Human Nectin-2/CD112 (2229-N2) binds with an ED50 of 0.150-0.750 μg/mL.
2 μg/lane of Recombinant Cynomolgus Monkey PVRIG Fc Chimera (Catalog # 10718-PV) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 52-63 kDa and 104-126 kda, respectively.
Human PVRIG (poliovirus receptor related immunoglobulin domain-containing protein), also known as CD112 receptor (CD112R), is an approximately 34 kDa single transmembrane protein in the poliovirus receptor-like protein (PVR) family (1). It is composed of a single extracellular IgV domain, one transmembrane domain, and a long intracellular domain. The intracellular domain contains two tyrosine residues, one within an ITIM-like motif that is a potential docking site for phosphatases (1). The extracellular domain sequence of cynomolgus monkey PVRIG have approximately 90% similarity with human PVRIG, respectively. The human PVRIG gene is preferentially expressed in lymphocytes, such as T cells and NK cells, but not in monocyte derived dendritic cells (1). PVRIG functions as a cell surface receptor for Nectin-2/CD112, a cell surface protein that is widely expressed on antigen-presenting cells and tumor cells. Disrupting the PVRIG/Nectin-2 interaction enhances human T cell response, suggesting PVRIG is a novel checkpoint for human T cells (1-3). Blocking PVRIG with neutralizing antibody is a feasible approach for NK cell mediated immunotherapy of cancers (4, 5).
- Zhu, Y. et al. (2016) J. Exp. Med. 213:167.
- Whelan, S. et al. (2019) Cancer Immunol Res. 7:257.
- Murter, B. et al. (2019) Cancer Immunol Res. 7:244.
- Li, J. et al. (2020) Haematologica. DOI:10.3324/haematol.2020.258574.
- Sanchez-Correa, B. et al. (2019) Cancers (Basel) 11:877.
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