Recombinant Cynomolgus Monkey PVRIG Fc Chimera Protein, CF

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.

• Reactivity: Pm-Cm
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Cynomolgus Monkey PVRIG Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey PVRIG Fc Chimera is immobilized at 1.00 µg/mL (100 µL/well), Recombinant Human Nectin-2/CD112 (Catalog # 2229-N2) binds with an ED₅₀ of 0.150-0.750 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived cynomolgus monkey PVRIG protein
  

  Cynomolgus Monkey PVRIG (Gly20, Ser21 or Glu23-Leu172) Accession # XP_005549281.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: XP_005549281.1
• N-terminal Sequence: Gly20, Ser21, Glu23
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 45 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 52-63 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Cynomolgus Monkey PVRIG Fc Chimera Protein, CF

• C7orf15
• C7orf15MGC138295
• CD112R
• MGC104322
• MGC138297
• MGC2463
• poliovirus receptor related immunoglobulin domain containing
• Poliovirus receptor-related immunoglobulin domain-containing protein
• PVRIG
• transmembrane protein PVRIG

Background

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).

1. Zhu, Y. et al. (2016) J. Exp. Med. 213:167.
2. Whelan, S. et al. (2019) Cancer Immunol Res. 7:257.
3. Murter, B. et al. (2019) Cancer Immunol Res. 7:244.
4. Li, J. et al. (2020) Haematologica. DOI:10.3324/haematol.2020.258574. 
5. Sanchez-Correa, B. et al. (2019) Cancers (Basel) 11:877.

Bioinformatics

• Uniprot:
  • XP_005549281.1()