Cat: IPD-X31110

Recombinant Staphylococcus aureus Peptide deformylase Protein,His & SUMO

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Analytical Data

  • 基因名

    Peptide deformylase

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    Polypeptide deformylase

  • 种属

    Staphylococcus aureus

  • 表达系统

    E. coli

  • 标签

    N- His-SUMO

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    P68826

  • 表达区间

    1-183aa

  • 分子量

    36.6 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

Peptide deformylase (PDF) is an essential bacterial enzyme that plays a crucial role in the co-translational processing of newly synthesized proteins by removing the N-formyl group from the N-terminus of formylmethionyl peptides. This enzymatic activity is vital for the maturation of proteins and is unique to prokaryotes, making PDF a potential target for antibiotic drug development. The increasing prevalence of antibiotic-resistant bacteria has intensified the search for novel therapeutic agents, with PDF emerging as a promising candidate due to its distinct mechanism of action. Research on recombinant PDF has gained momentum, focusing on its structure, function, and interaction with potential inhibitors. By producing recombinant PDF in suitable expression systems, researchers are able to study its catalytic properties in detail and assess the impact of various small molecules as inhibitors. This work not only deepens our understanding of bacterial protein synthesis but could also aid in the design of targeted inhibitors that circumvent existing resistance mechanisms. Overall, the exploration of recombinant peptide deformylase holds significant implications for microbiology and pharmaceutical development, offering new avenues for combating antibiotic resistance.

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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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