Recombinant Human BTLA Fc Chimera (aa 25-150) Protein, CF Summary
Product Specifications
Human BTLA Ile25-Ser150 Accession # AAP44003 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
8385-BT
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
When Recombinant Mouse HVEM/TNFRSF14 Fc Chimera (Catalog # 2516-HV) is immobilized at 0.5 µg/mL, Recombinant Human BTLA Fc Chimera binds with an ED50 of 0.25-1.25 µg/mL.
Reconstitution Calculator
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 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 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 (12).
- Murphy, K.M. et al. (2006) Nat. Rev. Immunol. 6:671.
- Croft, M. (2005) Trends. Immunol. 26:292.
- Watanabe, N. et al. (2003) Nat. Immunol. 4:670.
- Gavrieli, M. et al. (2003) Biochem. Biophys. Res. Commun. 312:1236.
- Chemnitz, J.M. et al. (2006) J. Immunol. 176:6603.
- Han, P. et al. (2004) J. Immunol. 172 :5931.
- Compaan, D.M. et al. (2005) J. Biol. Chem. 280:39553.
- Sedy, J. R. et al. (2005) Nat. Immunol. 6:90.
- Hurchla, M.A. et al. (2005) J. Immunol. 174:3377.
- Krieg, C. et al. (2007) Nat. Immunol. 8:162.
- Bekiaris, V. et al. (2013) Immunity 39:1082.
- Cai G and Freeman GJ, (2009) Immunol Rev. 229:244
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