Biotinylated BCMA Proteins
BCMA is selectively induced during plasma cell differentiation and is nearly absent on naive and memory B cells(Avery et al., 2003; Chiu et al., 2007). The interaction between BCMA and its ligand BAFF and APRIL is involved forthe maintenance of long-lived plasma cells (O’Connor et al., 2004; Peperzak et al., 2013). Multiple BCMA-targeted
therapies of B-cell derived malignancies are underdevelopment, including BCMA-targeting chimeric antigen
receptor T (CAR-T) and GlaxoSmithKline’s GSK2857916.

Selective interaction between BAFF/APRIL and theirLong-lived plasma cells

BAFFAPRIL

B cells

BAFFRreceptors. Note BCMA can interact with both BAFFand APRIL (Bolkun et al., 2016). The affinity ofAPRIL-BCMA interaction, however, is much higher
than that of BAFF-BCMA binding (Bossen andSchneider, 2006).

Mature B cells

BCMA

TACI

ACROBiosystems provides a comprehensive panel of BCMA proteins, including the exclusive biotinylated BCMA(Cat. # BC7-H82F0) and the monomeric BCMA (Cat. # BCA-H522y).

MoleculeCat. NoSpecies

BCMA (Biotin-labeled)

BC7-H82F0

HumanStructure
BCMA (1-54)

Fc

Avi

Immobilized Human BAFF, Fc Tag (Catalog # BAF-H4268)
at 5μg/mL (100 μL/well) can bind Biotinylated HumanBCMA, Fc Tag (Cat. # BC7-H82F0) with a linear range of
0.12-1.95 ng/mL.

Biotinylated BCMA Proteins
MoleculeCat. NoSpecies

BCMA

BCA-H522y

Human

The purity of Human BCMA, His Tag (Cat. # BCAH522y) is greater than 93% as determined by SECHPLC.

Structure
BCMA (1-54)

His

Immobilized Human BCMA, His Tag (Cat. # BCAH522y) at 5μg/mL (100 μL/well) can bind
Biotinylated Human BAFF (Cat. # BAF-H82Q2)
with a linear range of 0.24-3.9 ng/mL.

MoleculeCat. NoSpecies

Structure

BCMA (FITC)BCA-HF254

Human

BCMA (1-54)

Fc

BCMA

BC7-H5254

Human

BCMA (1-54)

Fc

BAFF

BAF-H4218

Human

BAFF (134-285)

BAFF

BAF-H4268

Human

Fc

BAFF (134-285)

BAFF

BAF-H5248

Human

His

BAFF (134-285)

BAFF (Biotin-labeled)BAF-H82F3

Human

Avi

Fc

BAFF (FITC)

BAF-HF268

Human

Fc

BAFF (134-285)

BAFF (Biotin-labeled)BAF-H82Q2

Human

His

Avi

BAFFR (Biotin-labeled)

BAR-M82F0

Mouse

BAFFR (10-71)

BAFF (134-285)

BAFF (134-285)
Fc

Avi

Coming soon
Biotinylated Cyno-BCMA & Biotinylated mouse BAFFR.
References
Avery, D.T., Kalled, S.L., Ellyard, J.I., Ambrose, C., Bixler, S.A., Thien, M., Brink, R., Mackay, F., Hodgkin, P.D., and Tangye, S.G.
(2003). BAFF selectively enhances the survival of plasmablasts generated from human memory B cells. J. Clin. Invest. 112,286–297.
Chiu, A., Xu, W., He, B., Dillon, S.R., Gross, J.A., Sievers, E., Qiao, X., Santini, P., Hyjek, E., Lee, J., et al. (2007). Hodgkin
lymphoma cells express TACI and BCMA receptors and generate survival and proliferation signals in response to BAFF andAPRIL. Blood 109, 729–739.
O’Connor, B.P., Raman, V.S., Erickson, L.D., Cook, W.J., Weaver, L.K., Ahonen, C., Lin, L.-L., Mantchev, G.T., Bram, R.J., andNoelle, R.J. (2004). BCMA Is Essential for the Survival of Long-lived Bone Marrow Plasma Cells. J. Exp. Med. 199, 91–98.
Peperzak, V., Vikström, I., Walker, J., Glaser, S.P., LePage, M., Coquery, C.M., Erickson, L.D., Fairfax, K., Mackay, F., Strasser,A., et al. (2013). Mcl-1 is essential for the survival of plasma cells. Nat. Immunol. 14, 290–297.
Bolkun, L., Grubczak, K., Schneider, G., Zembko, P., Radzikowska, U., Singh, P., Kloczko, J., Ratajczak, M.Z., Moniuszko, M.,and Eljaszewicz, A. (2016). Involvement of BAFF and APRIL in Resistance to Apoptosis of Acute Myeloid Leukemia. J. Cancer
7, 1979–1983.
Bossen, C., and Schneider, P. (2006). BAFF, APRIL and their receptors: structure, function and signaling. Semin. Immunol. 18,
263–275.

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