Recombinant Mouse CD6 His Tagged Protein, CF Summary
Details of Functionality |
Measured by the ability of the immobilized protein to support the adhesion of HuT 78 human cutaneous T cell lymphoma cells. The ED50 for this effect is 0.4-2.4 μg/mL.
|
Source |
Mouse myeloma cell line, NS0-derived mouse CD6 protein Leu18-Gly396, with a C-Terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Leu18 |
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 |
42 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 |
70-80 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 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 CD6 His Tagged Protein, CF
Background
CD6
is a member of the scavenger receptor cysteine-rich (SRCR) superfamily, which
is characterized by the presence of one or several repeats of SRCR domains in
their extracellular region (1). CD6 is a
type I transmembrane glycoprotein and contains three extracellular SRCR
domains (2, 3). It is expressed on thymocytes, T cells, a subset of B cells, and
on certain regions of the brain (3, 4). Mouse CD6 is a 665 amino acid
(aa) protein that includes a 16 aa signal sequence, a 382 aa extracellular
domain, a 21 aa transmembrane segment, and a 246 aa cytoplasmic region (5, 6). Within the ECD, mouse CD6 shares 69% and 88% aa sequence identity with human
and rat CD6, respectively. CD6
appears to play a role as both a co-stimulatory molecule in T cell activation
and as an adhesion receptor. Studies demonstrating a mitogenic effect for T cells with some CD6-specific monoclonal antibodies, in conjunction with either
accessory cells or PMA and anti-CD2 mAb, support the concept of CD6 as a
co-stimulatory molecule (7-12). Additionally, anti-CD6 monoclonal antibody
has been used as an immunosuppressive agent for patients undergoing kidney or
bone marrow allograft rejection. It has also been used to remove CD6
+ T cells
from donor bone marrow prior to allogenic bone marrow transplantation. Other
studies have demonstrated an adhesive role for CD6. It has been demonstrated to
bind the activated leukocyte cell adhesion molecule (ALCAM, CD166). CD6/ALCAM
interactions have been postulated to play a role in thymocyte development (9, 13). Additionally, the presence of ALCAM on neuronal cells may provide a
mechanism of interaction between CD6
+ T cell and ALCAM
+ neuronal cells.
Phosphorylation of the CD6 molecule appears to play a role in CD6-mediated
signal transduction (9, 13). Serine and threonine residues become
hyperphosphorylated and tyrosine residues become phosphorylated when T cells
are activated with anti-CD6 mAb in conjunction with PMA, anti-CD2, or anti-CD3
mAb (8, 10, 11, 14). The CD6 intracellular domain contains regions that can
interact with SH2 or SH3-containing proteins. However, the signaling pathways
have not been elucidated (5, 15, 16).
- Sarrias, M. et al. (2007) Proc. Natl. Acad. Sci. USA. 104:11724.
- Chappell, P. et al. (2015) Structure. 23:1426.
- Whitney, G.S. et al. (1995) J. Biol. Chem. 270:18187.
- Mayer, B. et al. (1990) J. Neuroimmunol. 29:193.
- Robinson, W.H. et al. (1995) J. Immunol. 155:4739.
- Aruffo, A. et al. (1997) Immunol. Today 18:498.
- Gangemi, R. et al. (1989) J. Immunol. 143:2439.
- Swack, J.A. et al. (1991) J. Biol. Chem. 266:7137.
- Starling, G.C. et al. (1996) Eur. J. Immunol. 26:738.
- Swack, J.A. et al. (1989) Mol. Immunol. 26:1037.
- Pawelec, G. and H.J. Buhring (1991) Human Immunol. 31:165.
- Singer, N.G. et al. (1996) Immunology 88:537.
- Degen, W.G. et al. (1998) Am. J. Pathol. 152:805.
- Osorio, L.M. et al. (1995) Cell Immunol. 166:44.
- Robinson, W.H. et al. (1995) Eur. J. Immunol. 25:2765.
- Whitney, G. et al. (1995) Mol. Immunol. 32:89.
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