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Recombinant Human BTLA Fc Chimera (aa 31-153) Protein, CF

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When Recombinant Mouse HVEM/TNFRSF14 Fc Chimera (Catalog # 2516-HV) iscoated at 0.5 µg/mL (100 μL/well), Recombinant Human BTLA Fc Chimera (Catalog #9509-BT) binds with an ED50 of 15-90 ng/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human BTLA Fc Chimera (aa 31-153) 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 Fc Chimera that produces 50% of the optimal binding response is 15-90 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human BTLA protein
Human BTLA
(Lys31-Trp153)
Accession # Q7Z6A9-1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Lys31
Structure / Form
Disulfide-linked homodimer
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
41 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
52-61 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 Fc Chimera (aa 31-153) 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), also known as B- and T-lymphocyte-associated protein and CD272, is a type I transmembrane glycoprotein that belongs to 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 domain, and a 111 aa cytoplasmic domain. The ECD of human BTLA shares 42% and 44% aa identity with mouse and rat BTLA, respectively. Unlike other CD28 family members, the BTLA Ig domain in the ECD is of the I-type rather than V-type (4). BTLA is expressed on T cells, B cells, macrophages, dendritic cells and NK cells (5). BTLA is also unusual in its interaction with the TNF superfamily member HVEM rather than with B7 family ligands (6). Its expression is low in naïve T cells and increases during antigen-specific induction of anergy. 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 (7). Under the control of ROR gamma t and IL-7, BTLA regulates the homeostasis and inflammatory responses of gamma δT cells (8). The binding of BTLA and HVEM does not preclude the concurrent binding of other HVEM ligands such as LIGHT or Lymphotoxin‑alpha (10).
  1. Murphy, K.M. et al. (2006) Nat. Rev. Immunol. 6:671.
  2. Croft, M. (2005) Trends. Immunol. 26:292.
  3. Watannabe, N. et al. (2003) Nat. Immunol. 4:670.
  4. Compaan, D.M. et al. (2005) J. Biol. Chem. 280:39553.
  5. Hurchia, M.A. et al. (2005) J. Immunol. 174:3377.
  6. Sedy, J. R. et al. (2005) Nat. Immunol. 6:90.
  7. Krieg, C. et al. (2007) Nat. Immunol. 8:162.
  8. Bekiaris, V. et al. (2013) Immunity 39:1082.
  9. Gavrieli, M. et al. (2003) Biochem. Biophys. Res. Commun. 312:1236.
  10. Cai G and Freeman GJ, (2009) Immunol Rev. 229:244

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