Recombinant Human B7-H4 Fc Chimera Biotinylated Protein, CF

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Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human B7-H4 Fc Chimera Biotinylated Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit anti-CD3 antibody induced IL-2 secretion in human T lymphocytes. The ED50 for this effect is 0.1-0.5 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human B7-H4 protein
Human B7-H4
(Phe29-Ala258)
Accession # Q7Z7D3
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Phe29
Structure / Form
Disulfide-linked homodimer. Biotinylated via sugars.
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

Theoretical MW
52 kDa (unlabeled).
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
81-94 kDa and 170 - 195 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 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 B7-H4 Fc Chimera Biotinylated Protein, CF

  • B7h.5
  • B7H4
  • B7-H4
  • B7H4T-cell costimulatory molecule B7x
  • B7S1
  • B7S1VCTN1
  • B7x
  • B7XPRO1291
  • FLJ22418
  • Immune costimulatory protein B7-H4
  • Protein B7S1
  • T cell costimulatory molecule B7x
  • V-set domain containing T cell activation inhibitor 1
  • V-set domain-containing T-cell activation inhibitor 1
  • Vtcn1

Background

B7-H4, also known as B7x and B7S1, is a 50-80 kDa glycosylated member of the B7 family of immunomodulatory proteins (1, 2). Mature human B7-H4 consists of a 235 amino acid (aa) extracellular domain (ECD) with one Ig-like V-set domain and one Ig-like C2-set domain, a 21 aa transmembrane segment, and a 2 aa cytoplasmic tail (3-5). Within the ECD, human B7-H4 shares 90% aa sequence identity with mouse and rat B7-H4. It shares 22% - 28% aa sequence identity with human B7-1, B7-2, B7-H1, B7-H2, B7-H3, and PD-L2. Alternate splicing of human B7-H4 generates an additional isoform that lacks the first Ig-like domain. B7-H4 is expressed on the surface of activated lymphocytes, macrophages, monocytes, dendritic cells, epithelial cells, and bone marrow-derived mesenchymal stem cells
(4-8). Its binding to activated T cells dampens T cell responses and induces cell cycle arrest in the T cell (3-5). Reverse signaling can induce either cell cycle arrest or apoptosis in the B7-H4 expressing cell (9, 10). B7-H4 is up-regulated in several carcinomas in correlation with tumor progression and metastasis (2, 7, 11, 12). A soluble form of B7-H4 is elevated in the serum of ovarian cancer, renal cell carcinoma, and rheumatoid arthritis patients, also in correlation with advanced disease status (13-15). Soluble B7-H4 functions as a decoy molecule that blocks the inhibitory influence of B7-H4 on immune activation (15). Despite evidence for the involvement of B7-H4 in immune regulation, mice deficient in its expression do not show significant immune deficiencies, suggesting compensation by other molecules in vivo (16).
  1. Yi, K.H. and L. Chen (2009) Immunol. Rev. 229:145.
  2. Salceda, S. et al. (2005) Exp. Cell Res. 306:128.
  3. Zang, X. et al. (2003) Proc. Natl. Acad. Sci. 100:10388.
  4. Prasad, V.R. et al. (2003) Immunity 18:863.
  5. Sica, G.L. et al. (2003) Immunity 18:849.
  6. Kryczek, I. et al. (2006) J. Exp. Med. 203:871.
  7. Tringler, B. et al. (2005) Clin. Cancer Res. 11:1842.
  8. Xue, Q. et al. (2010) Stem Cells Dev. 19:27.
  9. Song, H. et al. (2008) Cancer Lett. 266:227.
  10. Park, G.B. et al. (2009) Immunology 128:360.
  11. Zang, X. et al. (2007) Proc. Natl. Acad. Sci. 104:19458.
  12. Krambeck, A.E. et al. (2006) Proc. Natl. Acad. Sci. 103:10391.
  13. Simon, I. et al. (2006) Cancer Res. 66:1570.
  14. Thompson, R.H. et al. (2008) Cancer Res. 68:6054.
  15. Azuma, T. et al. (2009) PloS Med. 6:e1000166.
  16. Suh, W.-K., et al. (2006) Mol. Cell. Biol. 26:6403.

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