>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When
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.
Human embryonic kidney cell, HEK293-derived cynomolgus monkey PD-L2/B7-DC protein
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 of 0.1-0.6 μg/mL.
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).
Ceeraz, S. et al. (2013) Trends Immunol. 34:556.
Latchman, Y. et al. (2001) Nat. Immunol. 2:261.
Tseng, S.-Y. et al. (2001) J. Exp. Med. 193:839.
Messal, N. et al. (2011) Mol. Immunol. 48:2214.
Zuccarino-Catania, G.V. et al. (2014) Nat. Immunol. 15:631.
Guo, G. et al. (2012) Clin. Rheumatol. 31:271.
Loke, P. and J.P. Allison (2003) Proc. Natl. Acad. Sci. USA 100:5336.
Matsumoto, K. et al. (2004) J. Immunol. 172:2530.
Stanciu, L.A. et al. (2006) J. Infec. Dis. 193:404.
Lewkowich, I.P. et al. (2013) Mucosal Immun. 6:728.
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