# | Product Name | Applications | Reactivity | |
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89628 | Human BAFF/TNFSF13B (hBAFF) Recombinant Protein |
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Product Information
MW (kDa) | 16 |
Purity | >98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hBAFF. All lots are greater than 98% pure. |
Endotoxin | Less than 0.01 ng endotoxin/1 μg hBAFF. |
Activity | The bioactivity of recombinant hBAFF was determined in a cell proliferation assay using mouse splenic B cells. The ED50 of each lot is between 0.5-2 ng/ml. |
Molecular Formula | Recombinant hBAFF contains no "tags" and the nonglycosylated protein has a calculated MW of 15,489. DTT-reduced and non-reduced protein migrate as 16 kDa polypeptides. The expected amino-terminal AVQGP of recombinant hBAFF was verified by amino acid sequencing. |
Recombinant human BAFF (hBAFF) Ala134-Leu285 (Accession #NP_006564) was expressed in human 293 cells at Cell Signaling Technology.
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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