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

When Recombinant Rat PD‑L2/B7‑DC Fc Chimera (Catalog # 9994-PL) is coated at 1 μg/mL (100 μL/well), Recombinant Rat PD-1 Fc Chimera (Catalog # 9814-PD) binds with an ED50 of 0.01-0.08 μg/mL.

2 μg/lane of Recombinant Rat PD‑L2/B7‑DC was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 62-73 kDa and 120-150 kDa, respectively.

• Reactivity: Rt
• Applications: Bioactivity
• Format: Carrier-Free

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

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Rat PD‑L2/B7‑DC Fc Chimera is coated at 1 μg/mL (100 μL/well), the concentration of Recombinant Rat PD-1 Fc Chimera (Catalog # 9814-PD) that produces 50% optimal binding response is 0.01-0.08 μg/mL
• Source: Mouse myeloma cell line, NS0-derived rat PD-L2/B7-DC protein
  

  Rat PD-L2 (Leu20-Arg219) Accession # NP_001101052.2	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: NP_001101052.2
• 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: 62-73 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and EDTA with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Rat 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 Butyrophilin B7-DC, is a member of the B7 family of proteins that provide signals for regulating T-cell activation and tolerance (1). In humans, the mature 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, rat PD-L2 shares 71% and 95% aa sequence identity with human and mouse PD-L2, respectively. 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:
  • NP_001101052.2()