Cat: PA2000-2607

Recombinant E.coli aac Protein,His

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Analytical Data

  • 基因名

    aac

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    aac;Alpha-actinin-3

  • 种属

    E.coli

  • 表达系统

    E. coli

  • 标签

    His tag N-Terminus

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P29958

  • 表达区间

    35-214aa

  • 氨基酸序列

    GGYAALIRRASYGVPHITADDFGSLGFGVGYVQAEDNICVIAESVVTANGERSRWFGATGPDDADVRTTSSTQAIDDRVAERLLEGPRDGVRAPCDDVRDQMRGFVAGYNHFLRRTGVHRLTDPACRGKAWVRPLSEIDLWRTSWDSMVRAGSGALLDGIVAATPPTAAGPASAPEAPDA

  • 分子量

    35.1kDa

  • 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.

Quality inspection process

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Protein Description

AAC, or Amino Acid-Comparative, recombinant proteins have garnered significant attention in recent years due to their potential applications in various fields, including medicine, biotechnology, and pharmaceuticals. The primary aim of AAC research is to create proteins that can mimic or enhance the function of naturally occurring proteins, thereby offering innovative solutions for treating diseases and improving agricultural practices. By employing advanced recombinant DNA technology, researchers can manipulate genetic sequences to produce proteins with desired characteristics, such as increased stability, improved efficacy, or novel functions. This approach not only accelerates the process of protein discovery and optimization but also facilitates large-scale production, making them more accessible for industrial applications. Furthermore, the therapeutic potential of AAC recombinant proteins is being explored in the context of enzyme replacement therapy, monoclonal antibodies, and vaccine development. As a result, understanding the structure-function relationships of these proteins is crucial for designing targeted therapies. The continuous advancement in bioinformatics and structural biology tools, coupled with an increasing emphasis on personalized medicine, promises to expand the horizons of AAC recombinant protein research, paving the way for breakthroughs in disease management and treatment.

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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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