Cat: PA2000-1504

Recombinant Human PISD Protein,His

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关键信息

  • 基因名

    PISD

  • 应用

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    PISD;Phosphatidylserine decarboxylase proenzyme. mitochondrial

  • 种属

    Human

  • 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

    Q9UG56

  • 表达区间

    1-375aa

  • 氨基酸序列

    MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGALRPLSRVGWRPVSRVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL

  • 分子量

    56.0 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.

质检流程

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背景信息

Pseudomonas aeruginosa is a common opportunistic pathogen responsible for various infections, particularly in immunocompromised patients. One of the key factors contributing to its virulence is the presence of proteinase inhibitors, such as PISD (Pseudomonas Inhibitor of Serine Proteases D), which play a significant role in the bacterium's ability to evade host immune responses. Research on the PISD protein has gained traction due to its potential utility in therapeutic applications and as a target for novel antimicrobial strategies. Understanding the structure, function, and mechanisms of PISD can provide insights into its role in bacterial pathogenicity and immune evasion. Studies have demonstrated that PISD can inhibit various serine proteases, which are crucial in the activation of immune pathways. By exploring the biochemical properties and interactions of PISD with its substrates, researchers aim to elucidate the molecular pathways involved in bacterial resistance, which may pave the way for the development of innovative treatments against Pseudomonas infections. Moreover, characterizing PISD's structure could lead to the design of specific inhibitors that may assist in enhancing host defense mechanisms or restoring susceptibility to conventional antibiotics. This area of research is particularly relevant in the context of rising antibiotic resistance, making the exploration of protein-based approaches to combat infections a pressing imperative in modern medicine. Consequently, PISD not only serves as a fascinating subject for fundamental microbiological research but also represents a promising avenue for translational applications in the fight against antibiotic-resistant pathogens.

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