Recombinant Rat B7-2/CD86 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its ability to induce IL-2 secretion by Jurkat human acute T cell leukemia cells. Freeman, G.J. et al. (1993) Science 262:909. The ED50 for this effect is 0.075-0.3 µg/mL in the presence of PHA. |
Source |
Mouse myeloma cell line, NS0-derived rat B7-2/CD86 protein
Rat B7-2 (Val29-Ile250) Accession # O35531 |
IEGRMD |
Human IgG1 (Pro100-Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Val29 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Cd86 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
52 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 |
80-100 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 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 |
>95%, 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 Rat B7-2/CD86 Fc Chimera Protein, CF
Background
B7-2, also known as CD86, B70, and ETC-1, is a 60-100 kDa variably glycosylated protein in the B7 family. B7 family members are transmembrane cell surface molecules that play important roles in immune activation and the maintenance of immune tolerance (1, 2). Mature rat B7-2 consists of a 222 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 19 aa transmembrane segment, and a 46 aa cytoplasmic tail (3). Within the ECD, rat B7-2 shares 59% and 81% aa sequence identity with human and mouse B7-2, respectively. B7-2 is highly expressed on activated antigen presenting cells (APC),
e.g. B cells, dendritic cells, and monocytes (4-7), as well as on vascular endothelial cells (8). B7-2 and the closely related B7-1/CD80 exhibit overlapping but distinct functional properties. Their binding to CD28, which is constitutively expressed on T cells, enhances T cell receptor signaling and also provides TCR-independent co‑stimulation (4, 5, 7, 9‑12). B7‑1 and B7-2 additionally bind the CD28-related protein, CTLA-4, which is up‑regulated and recruited to the immunological synapse (IS) at the onset of T cell activation (4, 5, 7, 9‑11). CTLA-4 ligation inhibits the T cell response and supports regulatory T cell function (13). B7-2 is expressed earlier than B7-1 following APC activation (6), and both proteins bind with higher affinity to CTLA-4 than to CD28 (11). B7-2 promotes the stabilization of CD28 in the IS, while B7-1 is primarily responsible for promoting CTLA-4 recruitment and accumulation in the IS (14). The relative participation of B7-1 and B7-2 in T cell co-stimulation can also alter the Th1/Th2 bias of the immune response (15). Both B7-1 and B7-2 serve as cellular receptors for B species adenoviruses (16).
- Greenwald, R.J. et al. (2005) Annu. Rev. Immunol. 23:515.
- Bour-Jordan, H. et al. (2011) Immunol. Rev. 241:180.
- Maeda, K. et al. (1997) Int. Immunol. 9:993.
- Azuma, M. et al. (1993) Nature 366:76.
- Freeman, G.J. et al. (1993) J. Exp. Med. 178:2185.
- Lenschow, D.J. et al. (1993) Proc. Natl. Acad. Sci. USA 90:11054.
- Hathcock, K.S. et al. (1993) Science 262:905.
- Seino, K. et al. (1995) Int. Immunol. 7:1331.
- Freeman, G.J. et al. (1993) Science 262:909.
- Chen, C. et al. (1994) J. Immunol. 152:4929.
- Lanier, L.L. et al. (1995) J. Immunol. 154:97.
- Rudd, C.E. et al. (2009) Immunol. Rev. 229:12.
- Wing, K. et al. (2011) Trends Immunol. 32:428.
- Pentcheva-Hoang, T. et al. (2004) Immunity 21:401.
- Kuchroo, V.K. et al. (1995) Cell 80:707.
- Short, J.J. et al. (2006) Virus Res. 122:144.
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