Cat: IPD-X40329

Recombinant Aspergillus giganteus sar Protein ,His & Myc

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Analytical Data

  • 基因名

    sar

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    rRNA endonuclease

  • 种属

    Aspergillus giganteus

  • 表达系统

    E. coli

  • 标签

    N- His & C- Myc

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P00655

  • 表达区间

    28-177aa

  • 分子量

    25.2 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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Protein Description

SAR (Structure-Activity Relationship) protein reconstruction is an emerging area of research in the field of molecular biology and drug development. It focuses on understanding how the structural features of proteins correlate with their biological activity. This understanding is crucial for the design and optimization of pharmaceutical compounds. Historically, the development of drugs has been hindered by the lack of knowledge about protein structures and their functions, which can vary significantly even among closely related species. SAR studies involve the systematic alteration of protein structures to evaluate how these changes affect their interaction with potential drug molecules. Advanced techniques such as X-ray crystallography, NMR spectroscopy, and cryo-electron microscopy aid in elucidating protein structures in atomic detail, while computational tools facilitate the prediction of how modifications can enhance or inhibit protein function. Moreover, the integration of bioinformatics and machine learning is revolutionizing SAR research, allowing scientists to analyze large datasets and identify patterns that inform rational drug design. As a result, the study of SAR in proteins not only enhances our fundamental understanding of biological processes but also accelerates the development of targeted therapies for a range of diseases, including cancer, neurological disorders, and infectious diseases. This research is increasingly vital as the pharmaceutical industry seeks to develop more effective and personalized treatments, making SAR protein reconstruction a key focus for future innovations in drug discovery.

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IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
IPODIX North America (HQ)
Proteintech Group, Inc
5500 Pearl Street, Suite 400
Rosemont, IL 60018, USA
1-888-478-4522
proteintech@ptglab.com
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