Recombinant Human B7-H4 Fc Chimera Biotinylated Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. Biotinylated Recombinant Human B7‑H4 Fc Chimera binds to Human B7-H4 Antibody (Catalog # MAB6576) with an ED 50 of 1.50-15.0 ng/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-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Phe29 |
Structure / Form |
Disulfide-linked homodimer Biotinylated via amines |
Protein/Peptide Type |
Recombinant Proteins |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
52 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 |
75-95 kDa, under 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 with Trehalose. |
Reconstitution Instructions |
Reconstitute at 200 μg/mL in water. |
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
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).
- Yi, K.H. and L. Chen (2009)
Immunol. Rev. 229:145.
- Salceda, S. et al. (2005)
Exp. Cell Res. 306:128.
- Zang, X. et al.
(2003) Proc. Natl. Acad. Sci. 100:10388.
- Prasad, V.R. et al.
(2003) Immunity 18:863.
- Sica, G.L. et al.
(2003) Immunity 18:849.
- Kryczek, I. et al.
(2006) J. Exp. Med. 203:871.
- Tringler, B. et al.
(2005) Clin. Cancer Res. 11:1842.
- Xue, Q. et al.
(2010) Stem Cells Dev. 19:27.
- Song, H. et al.
(2008) Cancer Lett. 266:227.
- Park, G.B. et al.
(2009) Immunology 128:360.
- Zang, X. et al.
(2007) Proc. Natl. Acad. Sci. 104:19458.
- Krambeck, A.E. et al.
(2006) Proc. Natl. Acad. Sci. 103:10391.
- Simon, I. et al.
(2006) Cancer Res. 66:1570.
- Thompson, R.H. et al.
(2008) Cancer Res. 68:6054.
- Azuma, T. et al.
(2009) PloS Med. 6:e1000166.
- Suh, W.-K., et al.
(2006) Mol. Cell. Biol. 26:6403.
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