Recombinant Mouse PD-L2/B7-DC (K113S) Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Mouse PD‑L2/B7‑DC (K113S) Fc Chimera is immobilized at 2 µg/mL (100
µL/well),
Recombinant
Mouse RGM‑B (Catalog # 3597-RG)
binds with an ED 50 of 0.08-0.48 μg/mL. Recombinant Mouse PD‑L2/B7‑DC (K113S) Fc Chimera (Catalog #10021-PL) weakly binds to
Recombinant Mouse PD-1.
|
Source |
Mouse myeloma cell line, NS0-derived mouse PD-L2/B7-DC protein Mouse PD-L2 (Leu20-Arg219) (Lys113Ser) Accession # Q9WUL5 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
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 |
|
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 |
64-84 kDa, reducing conditions
|
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. - 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 PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse PD-L2/B7-DC (K113S) Fc Chimera Protein, CF
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, mouse PD-L2 shares 72% and 95% aa sequence identity with human
and rat 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 repulsive
guidance molecule family member b (RGMb) on macrophages and alveolar epithelial
cells, supporting respiratory immune tolerance (13). Replacement of lysine residue at position 113
with serine (K113S) has been reported to result in a loss of binding capacity
to PD-1, while retaining its T-cell stimulatory function through its
interaction with RGMb (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 (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.
- Nie, X. et al. (2017) Cell. Mol. Immunol. 14:1.
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