Recombinant Human BTLA His-tag Protein, CF

When Recombinant Mouse HVEM/TNFRSF14 Fc Chimera (Catalog # 2516-HV) is coated at 0.5 μg/mL, Recombinant BTLA (Catalog # 9235-BT) bindswith an ED50 of0.1-0.5 μg/mL.

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

Recombinant Human BTLA His-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse HVEM/TNFRSF14 Fc Chimera (Catalog # 2516-HV) is immobilized at 0.5 μg/mL, 100 μL/well, the concentration of Recombinant Human BTLA that produces 50% of the optimal binding response is approximately 0.1-0.5 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human BTLA protein
  Lys31-Leu150, with a C-terminal 6-His tag
• Accession #: NP_001078826.1
• N-terminal Sequence: Lys31
• 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: 15 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: 23-33 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 BTLA His-tag Protein, CF

• B and T lymphocyte associated
• B and T lymphocyte attenuator
• B- and T-lymphocyte attenuator
• B- and T-lymphocyte-associated protein
• BTLA
• BTLA1
• CD272 antigen
• CD272
• FLJ16065
• MGC129743

Background

B- and T-lymphocyte attenuator (BTLA; CD272) is a 35 kDa type I transmembrane glycoprotein in the CD28 family of T cell costimulatory molecules (1-3). Mature human BTLA contains a 127 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane sequence, and a 111 aa cytoplasmic domain. The two ITIM motifs and three Tyr phosphorylation sites in the cytoplasmic tail transmit inhibitory signaling (4-5). The ECD of human BTLA shares 42% and 44% aa identity with that of mouse and rat BTLA, respectively. A splice variant lacking the transmembrane domain has been reported (6). Unlike other CD28 family members, the BTLA Ig domain in the ECD is of the I-type rather than V-type, and BTLA does not form homodimers (7). BTLA is also unusual in its interaction with the TNF superfamily member HVEM rather than with B7 family ligands (8). BTLA is expressed on T cells, B cells, macrophages, dendritic cells, and NK cells (9). Its expression is low in naïve T cells and increases during antigen-specific induction of anergy. In B cells, BTLA expression is highest in mature naïve cells (9). BTLA apparently limits T cell numbers, since its deletion results in overproduction of T cells, especially CD8⁺ memory T cells that are hyper-responsive to TCR crosslinking (10). Under the control of ROR gamma t and IL-7, BTLA regulates the homeostasis and inflammatory responses of gamma δT cells (11). The binding of BTLA and HVEM does not preclude the concurrent binding of other HVEM ligands such as LIGHT or Lymphotoxin-alpha (12).

1. Murphy, K.M. et al. (2006) Nat. Rev. Immunol. 6:671.
2. Croft, M. (2005) Trends. Immunol. 26:292.
3. Watanabe, N. et al. (2003) Nat. Immunol. 4:670.
4. Gavrieli, M. et al. (2003) Biochem. Biophys. Res. Commun. 312:1236.
5. Chemnitz, J.M. et al. (2006) J. Immunol. 176:6603.
6. Han, P. et al. (2004) J. Immunol. 172 :5931
7. Compaan, D.M. et al. (2005) J. Biol. Chem. 280:39553.
8. Sedy, J. R. et al. (2005) Nat. Immunol. 6:90.
9. Hurchla, M.A. et al. (2005) J. Immunol. 174:3377.
10. Krieg, C. et al. (2007) Nat. Immunol. 8:162.
11. Bekiaris, V. et al. (2013) Immunity 39:1082.
12. Cai G and Freeman GJ, (2009) Immunol Rev. 229:244

Bioinformatics

• Uniprot:
  • NP_001078826.1()