Cat: PA2000-1762

Recombinant E.coli fno Protein,His

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Analytical Data

  • 基因名

    fno

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    fno;F420-dependent NADP reductase

  • 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

    D9PVP5

  • 表达区间

    1-224aa

  • 氨基酸序列

    MKIAVLGGTGDQGLGLALRLALAGEEVIIGSRDAEKAVSAAQKVLEIAERDDLKVKGATNAEAAEEAEVAILTVPLQAQMATLGSVKEAIKGKVLIDATVPIDSCLGGSAVRYIDLWDGSAAERAARFLEDQGTRVAAAFNNISASALLDITGPVDCDCLIASDHRDALDLASELAEKIDGVRAIDCGGLENARVIEKITPLLINLNIKNRIRNAGIRITNLPE

  • 分子量

    28.4 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.

Quality inspection process

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Protein Description

FNO (Fused Nucleotide Oligomerization) protein is an emerging focus of research in molecular biology due to its unique structural and functional properties. These proteins play critical roles in various biological processes, including signal transduction, cellular communication, and metabolic pathways. The study of FNO proteins has gained momentum as scientists seek to understand their mechanisms of action and potential applications in biotechnology and medicine. Recent advances in high-throughput sequencing and protein engineering techniques have enabled researchers to explore the diverse functions of FNO proteins in different organisms, revealing their involvement in disease pathways and cellular stress responses. Additionally, the potential for FNO proteins to serve as valuable tools for synthetic biology applications and therapeutic interventions has spurred interest in optimizing their stability and activity. Understanding the evolutionary relationships and functional diversity among FNO proteins is crucial for harnessing their capabilities in developing novel biocatalysts and targeted therapies. As research continues to uncover the intricate roles of FNO proteins, it holds promise for innovative solutions to some of the most pressing challenges in health and environmental sustainability.

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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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