Recombinant Human NTB-A/SLAMF6 His tag Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human NTB-A/SLAMF6 His tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human NTB-A/SLAMF6 is coated at 1 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human
  NTB-A/SLAMF6 Fc Chimera that produces 50% optimal binding response is 0.6-3 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human NTB-A/SLAMF6 protein
  Gln22-Met226, with a C-teminal 6-His tag
• Accession #: Q96DU3
• N-terminal Sequence: No results obtained. Gln22 inferred from enzymatic pyroglutamate treatment revealing Ser23
• 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: 24 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: 34-42 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 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 Human NTB-A/SLAMF6 His tag Protein, CF

• Activating NK receptor
• CD352 antigen
• CD352
• KALIFLJ50657
• Ly108
• NK-T-B-antigen
• NTBA receptor
• NTBA
• NTB-A
• NTB-AMGC104953
• NTBAT- and B-cell antigen
• SF2000
• SLAM family member 6
• SLAMF6

Background

NTB-A, also known as Ly108 and SLAMF6, is a 60 kDa type I transmembrane glycoprotein in the SLAM subgroup of the CD2 family (1). Mature human NTB-A consists of a 205 amino acid (aa) extracellular domain (ECD) with one Ig-like V-set and one Ig-like C2-set domain, a 21 aa transmembrane segment, and an 84 aa cytoplasmic domain with two immunoreceptor tyrosine-based switch motifs (ITSMs) (2, 3). An alternatively spliced isoform is truncated in the cytoplasmic domain and lacks the two ITSMs. Within the ECD, human NTB-A shares 48% aa sequence identity with mouse and rat NTB-A. The ECD of human NTB-A shares 19%-34% aa sequence identity with comparable regions of human 2B4, BLAME, CD2F-10, CD84, CD229, CRACC, and SLAM. NTB-A is expressed on the surface of NK, T, and B lymphocytes as well as eosinophils (2, 4, 5). It interacts homophilically through weak associations between the Ig-V domains (2, 5-7). NTB-A functions as an activating coreceptor on NK and T cells (2, 5, 6, 8). Tyrosine phosphorylation in the membrane proximal ITSM enables specific association with EAT-2, an interaction that is required for NTB-A mediated cytotoxicity of NK cells (9). Phosphorylation-dependent NTB-A association with SAP is required for full production of IFN-gamma by NK cells (5, 9). This interaction is independent of EAT-2 binding and appears to involve the membrane distal ITSM (5, 9). NTB-A deficient mice show weakened Th2 responses and elevated levels of neutrophil-derived inflammatory mediators (10). In B cells, NTB-A modulates immunoglobulin class switching and the balance between tolerance and autoimmunity (5, 11). In addition, NTB-A binds to the influenza virus hemagglutinin (HA) protein which co-stimulates NK cell activation (12). The Vpu protein encoded by HIV-1 interferes with NTB-A glycosylation and cell surface expression (13).

1. Claus, M. et al. (2008) Front. Biosci. 13:956.
2. Bottino, C. et al. (2001) J. Exp. Med. 194:235.
3. Fraser, C.C. et al. (2002) Immunogenetics 53:843.
4. Munitz, A. et al. (2005) J. Immunol. 174:110.
5. Valdez, P.A. et al. (2004) J. Biol. Chem. 279:18662.
6. Flaig, R.M. et al. (2004) J. Immunol. 172:6524.
7. Cao, E. et al. (2006) Immunity 25:559.
8. Stark, S. and C. Watzl (2006) Int. Immunol. 18:241.
9. Eissmann, P. and C. Watzl (2006) J. Immunol. 177:3170.
10. Howie, D. et al. (2005) J. Immunol. 174:5931.
11. Kumar, K.R. et al. (2006) Science 312:1665.
12. Duev-Cohen, A. et al. (2016) Oncotarget 7:13093.
13. Bolduan, S. et al. (2013) Virology 440:190.

Bioinformatics

• Uniprot:
  • Q96DU3()