Recombinant Mouse PD-L2/B7-DC His Tagged Protein, CF Summary
Leu20-Arg219, with a C-terminal 6-His tag
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 200 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 Mouse
PD-L2/B7-DC (Catalog #
9107-PL) is coated at 0.4 µg/mL, Recombinant Mouse PD-1 Fc Chimera (Catalog #
1021-PD) binds with a typical ED50 of 3-18 ng/mL.
Programmed Death Ligand 2 (PD-L2), also
known as B7-DC and butyrophilin-like protein, is a member of the B7 family of
proteins that provide signals for regulating T-cell activation and tolerance
(1). Mature mouse PD-L2 consists of a 199 amino acid (aa) extracellular domain
(ECD) with one V-like and one C-like Ig domain, a 23 aa transmembrane segment,
and a 5 aa cytoplasmic domain (2, 3). Within the ECD, mouse and human PD-L2
share 72% aa sequence identity. 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
upregulated 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.
- Ghiotto, M. et al. (2010) Int. Immunol. 22:651.
- Shin, T. et al. (2003) J. Exp. Med. 198:31.
- Xiao, Y. et al. (2014) J. Exp. Med. 211:943.
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