Cat: IPD-X40300

Recombinant Epstein-Barr virus BLLF1 Protein ,His & SUMO

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关键信息

  • 基因名

    BLLF1

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Membrane antigen Short name: MA

  • 种属

    Epstein-Barr virus

  • 表达系统

    E. coli

  • 标签

    N- His-SUMO

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P03200

  • 表达区间

    1-493aa

  • 分子量

    68.5 kDa

  • 内毒素

    < 1.0 EU per μg protein as determined by the LAL method.

  • 性状

    Freeze-dried powder

  • 缓冲液

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • 复溶方法

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • 个性化定制

    点位突变 标签定制 buffer定制 全长蛋白定制

  • 稳定性测试

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • 保存条件 & 期限

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • 运输条件

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

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背景信息

BLLF1, a protein derived from the Epstein-Barr virus (EBV), has garnered significant interest in the field of virology and immunology due to its role in modulating host immune responses. EBV, a member of the herpesvirus family, is associated with various diseases, including infectious mononucleosis and certain types of cancers, such as Burkitt lymphoma and nasopharyngeal carcinoma. The study of BLLF1 is particularly relevant as it is involved in the virus’s ability to evade the immune system, thereby facilitating persistent infections. Recent research has focused on the structural characterization of the BLLF1 protein and its interactions with host immune components, revealing its potential as a therapeutic target. Additionally, understanding the mechanisms by which BLLF1 influences immune evasion could lead to innovative approaches in the development of vaccines and treatments for EBV-associated diseases. The ongoing investigation into BLLF1’s role in viral pathogenesis underscores its significance in combating EBV-related disorders and enhancing our knowledge of herpesvirus biology.

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