Recombinant Human BAFF/BLyS/TNFSF13B (CHO-expressed), CF Summary
Details of Functionality |
Measured in a cell proliferation assay using anti-IgM stimulated mouse B cells. The ED50 for this effect is 0.2-1.2 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human BAFF/BLyS/TNFSF13B protein Ala134-Leu285 |
Accession # |
|
N-terminal Sequence |
Ala134 |
Structure / Form |
High Molecular Weight Multimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
TNFSF13B |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
17.0 kDa (monomer). 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 |
19 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 under reducing conditions and visualized by silver stain |
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 BAFF/BLyS/TNFSF13B (CHO-expressed), CF
Background
B-cell activating factor (BAFF), also known as BLyS, TALL-1, THANK, and TNFSF13B, is a 32 kDa transmembrane glycoprotein in the TNF ligand superfamily. It is involved in multiple aspects of immune system regulation, particularly towards B cells (1, 2). Mature human BAFF consists of a 46 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 218 aa extracellular domain (ECD) with a stalk region and one TNF-like domain (3, 4). Within aa 134-285 of the ECD, human BAFF shares 72% aa sequence identity with mouse BAFF. It can be expressed as a homo-oligomer or as a heteromer in association with the related TNFSF member APRIL (4, 5). A 18 kDa fragment containing the TNF-like domain can be released by proteolysis between Arg133 and Ala134 (4). Soluble BAFF is stored intracellularly in neutrophils and released upon inflammatory stimulation (6). Alternative splicing generates an isoform termed deltaBAFF that lacks 19 aa between the proteolytic cleavage site and the TNF-like domain. deltaBAFF can form heteromers with BAFF and negatively regulates BAFF function (7). BAFF is produced by many hematopoietic cell types including monocytes, macrophages, neutrophils, dendritic cells, and T cells and also by adipocytes (1, 2, 8). Both BAFF and APRIL are functional ligands for the TNF receptor superfamily members BCMA and TACI, and BAFF additionally binds and signals through BAFF R (9, 10). All three receptors are primarily expressed by B cells (10). BAFF plays a critical role in the development and survival of B lineage cells (2, 11, 12). Mice that overexpress BAFF exhibit elevated B cell numbers, increased formation and size of germinal centers, and symptoms of autoimmunity (13). Soluble BAFF is elevated in B cell malignancies, autoimmunity, and other immune disorders (1). In addition, BAFF co‑stimulates T cell activation, promotes a Th1 biased immune response, and promotes the expansion of Treg cells (14‑16). BAFF also promotes monocyte survival, proinflammatory cytokine secretion, and differentiation to macrophages (17).
- Lied, G.A. and A. Berstad (2011) Scand. J. Immunol. 73:1.
- Mackay, F. et al. (2010) Immunol. Rev. 237:205.
- Moore, P.A. et al. (1999) Science 285:260.
- Schneider, P. et al. (1999) J. Exp. Med. 189:1747.
- Roschke, V. et al. (2002) J. Immunol. 169:4314.
- Scapini, P. et al. (2003) J. Exp. Med. 197:297.
- Gavin, A.L. et al. (2003) J. Biol. Chem. 278:38220.
- Alexaki, V.-I. et al. (2009) J. Immunol. 183:5948.
- Yu, G. et al. (2000) Nat. Immunol. 1:252.
- Thompson, J.S. et al. (2001) Science 293:2108.
- Schiemann, B. et al. (2001) Science 293:2111.
- Litinskiy, M.B. et al. (2002) Nat. Immunol. 3:822.
- Batten, M. et al. (2000) J. Exp. Med. 192:1453.
- Huard, B. et al. (2001) J. Immunol. 167:6225.
- Sutherland, A.P.R. et al. (2005) J. Immunol. 174:5537.
- Walters, S. et al. (2009) J. Immunol. 182:793.
- Chang, S.K. et al. (2006) Blood 108:2687.
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