描述：
CST公司生产的人重组蛋白His6BAFF (hHis6BAFF) Ala134-Leu285 (Accession #NP_006564)是从人的293细胞表达而来。重组的hBAFF蛋白在N-末端有His6标签，蛋白分子量据推算为18,066Da。DTT-还原的蛋白和未还原的蛋白作为21kDa的蛋白而迁移。重组hHis6BAFF蛋白的N-末端序列通过测序得到。hHis6BAFF的生物活性是通过诱导小鼠脾细胞增值能力的实验来确定的。每个批次的ED50在0.5-2 ng/ml之间。每微克hHis6BAFF内毒素含量小于0.01 ng。
有载体: 每微克hHis6BAFF蛋白溶解在包含10 mM DTT和20 μg BSA的PBS（pH 7.2）溶液中，并通过 0.22 μm 滤膜冻干，胱氨酸不是生物活性所需要的。
无载体：每微克hHis6BAFF蛋白溶解在包含10 mM DTT的PBS（pH 7.2）溶液，并通过 0.22 μm 滤膜冻干，胱氨酸不是生物活性所需要的。
BAFF, TNF超家族的蛋白成员，是一个同源三聚体跨膜蛋白，经过剪切后可以形成可溶性的细胞因子(1)。BAFF 也能进一步的聚合形成60聚体结构(1)。BAFF在中性粒细胞、巨噬细胞、树突状细胞、活化的T细胞和上皮细胞中表达(1,2)。BAFF 在B细胞的发育、存活和激活中发挥了主要的作用(1,3,4)。BAFF结合到3个不同的受体上—BAFF-R、TACI 和 BCMA (1)。这些受体在B细胞及其谱系细胞的发育中具有不同的表达形式(1,2,4)。不像BAFF-R 和BCMA只结合到BAFF的三聚体形式上, TACI只能结合到细胞膜上或者BAFF更高级的结构上(1)。BAFF/ BAFF-R 的相互作用激活典型和非典型的NF-κB信号通路, PI3K/Akt 和 mTOR (2,4)。通过BAFF-R激活非典型的NF-κB信号通路受到TRAF3负调控(5)。研究表明BAFF水平的升高可能加剧许多自身免疫性疾病，这使得它成为治疗的理想靶标(2)。
原厂资料：
Source / Purification
Recombinant human His6BAFF (hHis6BAFF) Ala134-Leu285 (Accession #NP_006564) was expressed in human 293 cells at Cell Signaling Technology.
Molecular Characterization
Recombinant N-terminally His6-tagged hBAFF has a calculated MW of 18,066. DTT-reduced and non-reduced protein migrate as 21 kDa polypeptides. The expected amino terminus of recombinant hHis6BAFF was verified by amino acid sequencing.
Purity
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hHis6BAFF. All lots are greater than 98% pure.
Bioactivity
The bioactivity of recombinant hHis6BAFF was determined in a cell proliferation assay using mouse splenic B cells. The ED50 of each lot is between 0.5-2 ng/ml.
Endotoxin
Less than 0.01 ng endotoxin/1 μg hHis6BAFF.
Formulation
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 10 mM DTT and 20 μg BSA per 1 μg hHis6BAFF. Cystines are not required for bioactivity. Carrier free: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 10 mM DTT. Cystines are not required for bioactivity.
Background
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 signaling (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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