Detects human BAFF/BLyS/TNFSF13B in direct ELISAs and Western blots. In Western blots, approximately 5% cross‑reactivity with recombinant human (rh) TL1A/TNSF15 is observed and no cross-reactivity with rhAPRIL, rhTNF-alpha, rhFas Ligand, rhGITR Ligand, rhLIGHT, rhTRAIL, rhTRANCE, or rhTWEAK is observed.
Monoclonal Mouse IgG1 Clone # 137314
E. coli-derived recombinant human BAFF/BLyS/TNFSF13B Ala81-Leu285 Accession # Q9Y275
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
Human peripheral blood mononuclear cells treated with PMA and Ca2+ ionomycin, fixed with paraformaldehyde, and permeabilized with saponin
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
(also known as TALL-1, BLyS, and THANK) is a type II transmembrane
glycoprotein belonging to the TNF superfamily and has been designated as
TNF superfamily member 13B (TNFSF13B). Human BAFF is a 285 amino acid
(aa) protein consisting of a 218 aa extracellular domain, a 21 aa
transmembrane region and a 46 aa cytoplasmic tail (1, 2). BAFF has the
typical structural characteristics of the TNF superfamily ligands. It is
a homotrimeric protein having the structurally conserved motif known as
TNF homology domain (3, 4). A higher ordered structure composed of a
cluster of trimeric units resembling the structure of a viral capsid has
also been reported (4). Human BAFF may be shed from the cell surface by
proteolytic cleavage between R133 and Ala134 to yield a soluble form of
the protein that is detectable in serum (1, 5). Within the TNF
superfamily BAFF shares the highest homology (48%) with APRIL (1). BAFF
shares with APRIL the ability to bind to BCMA and TACI and also binds
specifically to BAFF receptor (BAFF R, also known as BR3 or TNFSFR13C),
which is the principal BAFF receptor (6 - 8). All three receptors are
type III transmembrane proteins that are expressd in B cells. BAFF and
APRIL can form active heteromers that bind to TACI (9). BAFF is
expressed in peripheral blood mononuclear cells, in spleen and lymph
nodes. Its expression in resting monocytes is up-regulated by IFN-alpha,
IFN-beta, LPS and IL-10. BAFF provides critical survival signals to a
subset of B cells with intermediate maturation status (T2 B cells)
during the immune response (10). BAFF also plays an important role in
the development of lymphoid tissue and enhances the survival of
activated memory B cells (7, 11). Human and mouse BAFF share 86% aa
sequence identity (1).
Schneider, P. et al. (1999) J. Exp. Med. 189:1747.
Mukhopadhyay, A. et al. (1999) J. Biol. Chem. 274:15978.
Karpusas, M. et al. (2002) J. Mol. Biol. 315:1145.
Liu, Y. et al. (2002) Cell 108:383.
Cheema, G.S. et al. (2001) Arthr. Rheum. 44:1313.
Marsters, S.A. et al. (2000) Curr. Biol. 10:785.
Thompson, J.S. et al. (2001) Science 293:2108.
Ng, L.G. et al. (2004) J. Immunol. 173:807.
Roschke, V. et al. (2002) J. Immunol. 169:4314.
Batten, M. et al. (2000) J. Exp. Med. 192:1453.
Avery, D.T. et al. (2003) J. Clin. Invest. 112:286.
B cell Activating Factor
Entrez Gene IDs:
10673 (Human); 24099 (Mouse); 498666 (Rat)
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
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