Recombinant Cynomolgus PD-L2/B7-DC Fc Chimera Protein, CF

When Recombinant Human PD-1 Fc Chimera (Catalog #1086-PD) is coated at 1 µg/mL (100 μL/well), Recombinant Cynomolgus Monkey PD‑L2/B7‑DC Fc Chimera (Catalog # 9178-PL) binds with a typical ED50 of0.1-0.6 μg/mL.

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

Recombinant Cynomolgus PD-L2/B7-DC Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human PD-1 Fc Chimera (Catalog # 1086-PD) is immobilized at 1 μg/mL, 100 μL/well, the concentration of Recombinant Cynomolgus Monkey PD‑L2/B7‑DC Fc Chimera that produces 50% of the optimal binding response is approximately 0.1-0.6 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived cynomolgus monkey PD-L2/B7-DC protein
  

  Cynomolgus Monkey PD-L2/B7-DC (Leu20-Pro219) Accession # XP_005581839	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: XP_005581839
• N-terminal Sequence: Leu20
• 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: 49 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: 62-77 kDa, 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 100 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 PD-L2/B7-DC Fc Chimera Protein, CF

• B7-DC
• bA574F11.2
• Btdc
• Butyrophilin B7-DC
• Butyrophilin-like Protein
• CD273 antigen
• CD273
• CD273PD-1 ligand 2
• MGC142240
• PD-1-ligand 2
• PDCD1L2MGC142238
• PDCD1LG2
• PDL2
• PD-L2
• PDL2B7DC
• PD-L2PDCD1 ligand 2
• programmed cell death 1 ligand 2
• Programmed death ligand 2

Background

Programmed Death Ligand 2 (PD-L2), also known as B7-DC and butyrophilin-like protein, is a transmembrane member of the B7 family of proteins that provide signals for regulating T-cell activation and tolerance (1). Within the ECD, cynomolgous PD-L2 shares 71% and 96% aa sequence identity with mouse and human PD-L2, respectively (2, 3). PD-L2 is expressed on dendritic cells, subsets of activated CD4⁺ and CD8⁺ T cells, and memory B cells that differentiate into plasma cells (3-5). At inflammatory sites such as rheumatoid arthritis, allergen exposure, and virus infection, PD-L2 is up-regulated on synoviocytes, infiltrating macrophages, dendritic cells, and airway epithelial cells (6-10). PD-L2, along with B7-H1/PD-L1, binds to T cell PD-1 where it promotes IFN-gamma production and CD40 Ligand up-regulation while inhibiting IL-4 production (2, 3, 11, 12). In addition, PD-L2 binds to RGM-B on macrophages and alveolar epithelial cells, supporting respiratory immune tolerance (13). In asthma, PD-L2 suppresses IL-5 and IL-13 production, promotes IL-12 production by dendritic cells, and supports allergen-induced airway hyper-responsiveness and mucus production (8, 10).

1. Ceeraz, S. et al. (2013) Trends Immunol. 34:556.
2. Latchman, Y. et al. (2001) Nat. Immunol. 2:261.
3. Tseng, S.-Y. et al. (2001) J. Exp. Med. 193:839.
4. Messal, N. et al. (2011) Mol. Immunol. 48:2214.
5. Zuccarino-Catania, G.V. et al. (2014) Nat. Immunol. 15:631.
6. Guo, G. et al. (2012) Clin. Rheumatol. 31:271.
7. Loke, P. and J.P. Allison (2003) Proc. Natl. Acad. Sci. USA 100:5336.
8. Matsumoto, K. et al. (2004) J. Immunol. 172:2530.
9. Stanciu, L.A. et al. (2006) J. Infec. Dis. 193:404.
10. Lewkowich, I.P. et al. (2013) Mucosal Immun. 6:728.
11. Ghiotto, M. et al. (2010) Int. Immunol. 22:651.
12. Shin, T. et al. (2003) J. Exp. Med. 198:31.
13. Xiao, Y. et al. (2014) J. Exp. Med. 211:943.

Bioinformatics

• Uniprot:
  • XP_005581839()