• Purity

  >85%, by SDS-PAGE with silver staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When Recombinant Mouse HVEM/TNFRSF14 Fc Chimera (Catalog # ) is immobilized at 0.5 μg/mL (100 μL/well), the concentration of Recombinant Human BTLA Fc Chimera that produces 50% of the optimal binding response is approximately 0.25-1.25 μg/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Human BTLA Ile25-Ser150 Accession # AAP44003	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Ile25

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  41 kDa

• SDS-PAGE

  53-65 kDa, reducing conditions

Background: BTLA

B- and T-lymphocyte attenuator (BTLA; CD272) is a 35 kDa type I transmembrane glycoprotein in the CD28 family of T cell co-stimulatory 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 na?ve T cells and increases during antigen-specific induction of anergy. In B cells, BTLA expression is highest in mature na?ve 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 cross-linking (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 (4).

• References:

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.

• Long Name:

  B- And T-Lymphocyte Attenuator

• Entrez Gene IDs:

  151888 (Human); 208154 (Mouse)

• Alternate Names:

  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