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Recombinant Mouse CD8 alpha/beta Heterodimer Protein, CF

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Recombinant Mouse CD8 alpha/beta (Catalog # 11146-CD) has a molecular weight (MW) of 65.7 kDa as analyzed by SEC-MALS, suggesting that this protein is a heterodimer.  MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).
Recombinant Mouse CD8 alpha/beta (Catalog # 11146-CD) has a molecular weight (MW) of 65.7 kDa as analyzed by SEC-MALS, suggesting that this protein is a heterodimer.  MW may differ from predicted MW due to ...read more
Recombinant Mouse CD8 alpha/beta Heterodimer Protein (Catalog # 11146-CD) supports the adhesion of Jurkat human acute T cell leukemia cells. The ED50 for this effect is 0.750-6.00 μg/mL.

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse CD8 alpha/beta Heterodimer Protein, CF Summary

Additional Information
Analyzed by SEC-MALS.
Details of Functionality
Measured by its ability of the immobilized protein to support the adhesion of Jurkat human acute T cell leukemia cells. The ED50 for this effect is 0.750-6.00 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived mouse CD8 protein
Mouse CD8 alpha
(Lys28-Tyr196)
Accession # NP_033987.1		Acidic Tail6-His tag
Mouse CD8 beta
(Leu22-Thr175)
Accession # P10300.1		Basic TailFLAG
(DYKDDDDK)
N-terminusC-terminus
N-terminal Sequence
Lys28 (CD8 alpha) & Leu22 (CD8 beta)
Structure / Form
Disulfide-linked heterodimer
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
28 kDa (CD8 alpha) & 27 kDa (CD8 beta).
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
33-37 kDa & 45-51 kDa, under 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 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 PBS.

Notes

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

Alternate Names for Recombinant Mouse CD8 alpha/beta Heterodimer Protein, CF

  • CD_antigen: CD8a
  • CD8 antigen, alpha polypeptide (p32)
  • CD8
  • CD8a molecule
  • CD8A
  • Leu2 T-lymphocyte antigen
  • LEU2
  • MAL
  • OKT8 T-cell antigen
  • p32
  • T cell co-receptor
  • T8 T-cell antigen
  • T-cell antigen Leu2
  • T-cell surface glycoprotein CD8 alpha chain
  • T-lymphocyte differentiation antigen T8/Leu-2

Background

CD8, also known as Ly2 or Leu2, is a heterodimeric glycoprotein (alpha and beta subunits) that functions in conjunction with the T cell receptor in the recognition of MHC class I/peptide complexes (1, 2). CD8 alpha is expressed on double positive (CD4+ CD8+) thymocytes and mature CD8+ cytolytic T cells (CTL) (3-5), intraepithelial lymphocytes (IEL) (6), some gamma δ T cells (7), subsets of thymic and splenic dendritic cells (DC) (8), and peritoneal mast cells (9). It can form disulfide linked homodimers or heterodimers with CD8 beta (10). Thymic CD8+ DC express primarily alpha beta  heterodimers, while splenic CD8+ DC primarily express alpha alpha  homodimers (8). CD8 alpha + DC can present viral antigenic peptides in complex with MHC I and prime CTL responses (11). 
  1. Laugel, B. et al. (2011) J. Leukoc. Biol. 90:1089.
  2. Cole, D.K. et al. (2012) Immunology 137:139.
  3. Germain, R.N. (2002) Nat. Rev. Immunol. 2:309.
  4. Ledbetter, J.A. et al. (1980) J. Exp. Med. 152:280.
  5. Nakayama, K. et al. (1994) Science 263:1131.
  6. Wang, J. and J.R. Klein (1994) Science 265:1860.
  7. MacDonald, H.R. et al. (1990) Eur. J. Immunol. 20:927.
  8. Vremec, D. et al. (1992) J. Exp. Med. 176:47.
  9. Lin, T.J. et al. (1998) J. Immunol. 161:6265.
  10. Snow, P.M. and C. Terhorst (1983) J. Biol. Chem. 258:14675.
  11. Belz, G.T. et al. (2004) J. Immunol. 172:1996.

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