Recombinant Human PD-L2/B7-DC Fc protein (Catalog # 1224-PL) was immobilized on a Biacore Sensor Chip CM5, and binding to Recombinant Human PD-1 His protein (8986-PD) was measured at a concentration range between 6.0 nM ...read more
Recombinant Human PD-L2/B7-DC Fc Chimera (Catalog # 1224-PL) has a molecular weight (MW) of 120.3 kDa as analyzed by SEC-MALS, suggesting that this protein is a homodimer. MW may differ from predicted MW due to ...read more
Recombinant Human PD-L2/B7-DC Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized recombinant human (rh) PD-L2 at 1 µg/mL (100 µL/well) can bind rhPD-1 with a linear range of 7.5-500 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human PD-L2/B7-DC protein
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
49 kDa (monomer). 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
70-80 kDa, reducing conditions
Publications
Read Publications using 1224-PL in the following applications:
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.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human 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 member of the B7 family of proteins that provide signals for regulating T-cell activation and tolerance (1). Mature human PD-L2 consists of a 201 amino acid (aa) extracellular domain (ECD) with one V-like and one C-like Ig domain, a 21 aa transmembrane segment, and a 32 aa cytoplasmic domain (2, 3). Within the ECD, mouse and human PD-L2 share 72% aa sequence identity. Alternative splicing generates additional isoforms that lack the second Ig-like domain and may be substituted and truncated following the first Ig-like domain (4). 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, 6). 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 (7-11). 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, 12, 13). In addition, PD-L2 binds to RGM-B on macrophages and alveolar epithelial cells, supporting respiratory immune tolerance (14). 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 (9, 11).
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.
He, X.-H. et al. (2004) Acta Biochim. Biophys. Sinica 36:284.
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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