Recombinant Human SLAM/CD150 Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. Recombinant Human SLAM/CD150 binds to Biotinylated Recombinant Human SLAM/CD150 with an ED50 of 0.0400-0.400 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived human SLAM/CD150 protein Ala21-Lys236 with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ala21 & Thr25 |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
SLAMF1 |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
25 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 |
40-65 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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 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 Human SLAM/CD150 Protein, CF
Background
The type I transmembrane glycoprotein Signaling Lymphocytic Activation Molecule (SLAM), also known as CD150, is the prototypic member of the SLAM subfamily of the CD2 protein family. CD2 family proteins function as adhesion molecules and modulators of the immune response (1). Mature human SLAM consists of a 217 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and a 77 aa cytoplasmic domain with three immunoreceptor tyrosine switch motifs (ITSM) (2). Within the ECD, human SLAM shares 58% and 56% aa sequence identity with mouse and rat SLAM, respectively. Alternative splicing generates two additional isoforms, with one showing a deletion in the cytoplasmic region (aa 299-335), and a second showing a deletion in the transmembrane domain (aa 234-263). It is expressed as a 75 kDa molecule, of which approximately 30 kDa represents N-linked carbohydrate (3). SLAM is expressed on T cells, B cells, thymocytes, macrophages, dendritic cells, platelets, and hematopoietic stem cells, and it is up-regulated on activated B cells and CD4
+ and CD8
+ T cells (2‑8). SLAM interacts homophilically with low affinity, and this interaction induces a Th0/Th1 phenotype in CD8
+ T cells that is characterized by clonal expansion, production of IFN-gamma , and increased cytolytic activity (2, 3, 9-11). In addition, this interaction on CD4
+ T cells promotes a Th2-type response, likely due to an association with the adaptor molecule SAP (4, 12). SLAM ligation also promotes an allergen-induced eosinophil and mast cell activation, NKT cell development, and the microbicidal response of macrophages to Gram negative bacteria (8, 13-15). In humans, SLAM functions as a cellular entry receptor for measles virus (16, 17).
- Cannons, J.L. et al. (2011) Annu. Rev. Immunol. 29:665.
- Cocks, B.G. et al. (1995) Nature 376:260.
- Castro, A.G. et al. (1999) J. Immunol. 163:5860.
- Wang, N. et al. (2004) J. Exp. Med. 199:1255.
- Hahm, B. et al. (2004) Virology 323:292.
- Nanda, N. et al. (2005) Blood 106:3028.
- Kiel, M.J. et al. (2005) Cell 121:1109.
- Punnonen, J. et al. (1997) J. Exp. Med. 185:993.
- Mavaddat, N. et al. (2000) J. Biol. Chem. 275:28100.
- Aversa, G. et al. (1997) J. Immunol. 158:4036.
- Mehrle, S. et al. (2008) Mol. Immunol. 45:796.
- Davidson, D. et al. (2004) Immunity 21:707.
- Wang, N. et al. (2006) Am. J. Respir. Cell Mol. Biol. 35:206.
- Jordan, M.A. et al. (2011) J. Immunol. 186:3953.
- Berger, S.B. et al. (2010) Nat. Immunol. 11:920.
- Tatsuo, H. et al. (2000) Nature 406:893.
- Hsu, E.C. et al. (2001) Virology 279:9.
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