• Purity

  >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When Recombinant Human PD-1 Fc Chimera (Catalog # ) 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 (Leu20-Pro219) Accession # XP_005581839	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Leu20

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  49 kDa

• SDS-PAGE

  62-77 kDa, reducing conditions

Data Images

Background: PD-L2/B7-DC

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).

• References:

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.

• Long Name:

  Programmed Death-1 Ligand-2

• Entrez Gene IDs:

  80380 (Human); 58205 (Mouse); 102146227 (Cynomolgus Monkey)

• Alternate Names:

  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