Less than 1.0 EU/ug as determined by LAL method.
(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
Activity
Measured by its binding ability in a functional ELISA. Immobilized BCMA at 2 μg/ml can bind Anti-BCMA recombinant antibody, the EC50 of human BCMA protein is 1.912-2.488 ng/ml.
Measured by its binding ability in a functional ELISA. Immobilized TNFSF13B (CSB-MP897523HU1) at 10 μg/ml can bind human BCMA, the EC50 of human BCMA protein is 221.3-298.6 ng/ml.
Human TNFSF13B protein Fc tag (CSB-MP897523HU1) captured on COOH chip can bind Human BCMA protein Fc tag (CSB-MP023974HU1) with an affinity constant of 39 nM as detected by LSPR Assay.
BCMA (TNFRSF17/CD269) is a critical therapeutic target in multiple myeloma, and this recombinant construct covers the extracellular ligand-binding domain (residues 1–54) fused to a C-terminal hFc1 tag, providing the minimal receptor architecture necessary for ligand and antibody interaction studies. Functional ELISA validation demonstrates that immobilized BCMA at 2 μg/ml binds anti-BCMA recombinant antibody with an EC50 of 1.912–2.488 ng/ml, confirming conformational integrity suitable for therapeutic antibody epitope mapping, blocking antibody screening, and affinity characterization by SPR or BLI. Mammalian cell expression ensures native-like glycosylation and proper disulfide bond formation within this cysteine-rich domain, which supports use in receptor-ligand interaction assays and as a positive control in binding studies for biologic inhibitor discovery. Purity exceeding 90% by SDS-PAGE combined with endotoxin levels below 1.0 EU/μg satisfies the criteria typical for cell-based functional assays in immuno-oncology research.
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