Cat: IPD-X40396

Recombinant Naja mossambica mocarhagin Protein ,His

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Analytical Data

  • 基因名

    mocarhagin

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Zinc metalloproteinase mocarhagin

  • 种属

    Naja mossambica

  • 表达系统

    E. coli

  • 标签

    N- His

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    Q10749

  • 表达区间

    192-609aa

  • 分子量

    50.7 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

Mocarhagin is a recombinant protein derived from the venom of certain snake species, particularly known for its potential therapeutic applications. Research into mocarhagin has gained momentum due to its unique structure and biological activities, particularly its anticoagulant properties, which make it a promising candidate for the development of novel anticoagulant drugs. Traditional anticoagulant therapies often have limitations, such as risk of bleeding or the need for frequent monitoring, which has spurred interest in alternative agents like mocarhagin. Studies have shown that mocarhagin acts through specific mechanisms that inhibit blood clot formation while maintaining hemostasis, making it a safer option. The recombinant production of mocarhagin in laboratory settings presents advantages in terms of yield, purity, and reproducibility compared to extraction from natural sources. Furthermore, the insights gained from understanding its interaction with coagulation factors could lead to the design of more targeted therapies for a range of thrombotic disorders. Ongoing research is focused on elucidating the detailed mechanisms of mocarhagin's action, assessing its efficacy in preclinical models, and exploring its potential in clinical settings. The promising findings thus far highlight mocarhagin as a significant player in the field of anticoagulant research, with the potential to address limitations of current therapies and improve patient outcomes in thromboembolic diseases.

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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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