Cat: IPD-X40145

Recombinant Rhizomucor miehei Lipase Protein ,His

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Analytical Data

  • 基因名

    Lipase

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Lipase; EC 3.1.1.3; Triacylglycerol lipase

  • 种属

    Rhizomucor miehei

  • 表达系统

    E. coli

  • 标签

    N- His

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P19515

  • 表达区间

    25-363aa

  • 分子量

    40.8 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

Lipase, a crucial enzyme involved in lipid metabolism, catalyzes the hydrolysis of triglycerides into glycerol and free fatty acids, playing a significant role in various biological processes. The increasing demand for lipases in industrial applications, including food processing, pharmaceuticals, and biofuels, has driven extensive research into their properties and functions. The development of recombinant lipases has emerged as a promising strategy to enhance their yield, stability, and specificity. By utilizing recombinant DNA technology, scientists can produce lipase proteins in host organisms such as bacteria, yeast, or mammalian cells, allowing for high-level expression and easy purification. Moreover, the genetic modification of lipases can lead to improved enzymatic characteristics, enabling them to function under extreme conditions, such as high temperatures or varying pH levels, which are often required in industrial processes. Research in this area not only aims to optimize lipase production but also to explore the structure-function relationship of these enzymes, which can offer insights into their catalytic mechanisms. As the understanding of lipase structure and function advances, it opens new avenues for the development of customized lipase variants tailored for specific applications, thus contributing to innovations in biotechnology and sustainable practices.

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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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