RPMI 8226 cells were cultured with 0 to 500 ng/mL of hBAFF in the presence of 0.1 μM dexamethasone. Cell proliferation was assessed after 91 hours by measuring the OD490.
The purity of recombinant hBAFF was determined by SDS-PAGE of 1.5 µg reduced (+) and non-reduced (-) recombinant hBAFF and staining overnight with Coomassie Blue.
Recombinant human BAFF is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long term storage.
A greater than 90% purity was determined by SDS-PAGE.
Less than or equal to 1 EU / 1 μg hBAFF.
Recombinant human BAFF was expressed in E. coli and is supplied in a lyophilized form.
BAFF, a member of the TNF superfamily of proteins, is a homotrimeric transmembrane protein, which is cleaved to produce a soluble cytokine (1). BAFF may also further oligomerize into 60-mer structures (1). BAFF is expressed by neutrophils, macrophages, dendritic cells, activated T cells, and epithelial cells (1,2). BAFF plays a key role in B cell development, survival, and activation (1,3,4). BAFF binds to three distinct receptors, BAFF-R, TACI, and BCMA (1). These receptors are differentially expressed during B cell development and among B cell subsets (1,2,4). While BAFF-R and BCMA bind to the homotrimeric form of BAFF, TACI only binds to membrane bound or higher order BAFF structures (1). The BAFF/ BAFF-R interaction activates both canonical and non-canonical NF-κB pathways, PI3K/Akt, and mTOR (2,4). Activation of the noncanonical NF-κB pathway via BAFF-R is negatively regulated by TRAF3 (5). Elevated levels of BAFF may exacerbate many autoimmune disorders, making it an attractive therapeutic target (2).
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