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.
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.
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.
Recombinant human BAFF was expressed in E. coli and is supplied in a lyophilized form. A greater than 90% purity was determined by SDS-PAGE. Endotoxin levels are less than or equal to 1 EU / 1 μg hBAFF.
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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