>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
Bioactivity
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
Publications
Read Publication using 7537-BF in the following applications:
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 BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.
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) Protein
ApoL related ligand TALL-1
B lymphocyte stimulator
BAFF
BAFFB-cell activating factor
B-cell-activating factor
BLyS
BLYSB-lymphocyte stimulator
CD257 antigen
CD257
Dendritic cell-derived TNF-like molecule
DTL
TALL1
TALL-1delta BAFF
TALL1Delta4 BAFF
THANK
TNF- and APOL-related leukocyte expressed ligand 1
TNF and ApoL-related leukocyte expressed ligand 1
TNF homolog that activates apoptosis
TNFSF13B
TNFSF20
tumor necrosis factor (ligand) superfamily, member 13b
tumor necrosis factor (ligand) superfamily, member 20
tumor necrosis factor ligand superfamily member 13B
tumor necrosis factor superfamily, member 13b
tumor necrosis factor-like protein ZTNF4
ZTNF4
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.
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