Cat: PA2000-8377

Recombinant Human HSPC111 Protein,GST

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Analytical Data

  • 基因名

    HSPC111

  • Application

    SPRMSTBLIITCELISA细胞实验药物筛选

  • 别名

    CGI 117; HBV pre S2 trans regulated protein 3; HBV pre-S2 trans-regulated protein 3; HSPC185; Hypothetical protein HSPC111; NOP16; NOP16 Gene; NOP16 nucleolar protein homolog ; NOP16 nucleolar protein homolog (yeast); NOP16_HUMAN

  • 种属

    Human

  • 表达系统

    E. coli

  • 标签

    GST-tag at N-terminal

  • 纯度

    Greater than 90% as determined by SDS-PAGE.

  • 蛋白编号

    Q9Y3C1

  • 表达区间

    1-178aa

  • 氨基酸序列

    MPKAKGKTRRQKFGYSVNRKRLNRNARRKAAPRIECSHIRHAWDHAKSVRQNLAEMGLAVDPNRAVPLRKRKVKAMEVDIEERPKELVRKPYVLNDLEAEASLPEKKGNTLSRDLIDYVRYMVENHGEDYKAMARDEKNYYQDTPKQIRSKINVYKRFYPAEWQDFLDSLQKRKMEVE

  • 分子量

    45.32 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

HSPC111, also known as Heat Shock Protein Candidate 111, has garnered attention in the field of molecular biology and biomedicine due to its involvement in cellular stress responses and its potential implications in various diseases. Heat shock proteins (HSPs) play crucial roles in protein folding, protecting cells from stress-induced damage, and facilitating recovery from physiological insults. The HSPC111 protein is categorized within the larger family of HSPs and is believed to participate in crucial cellular processes, including protein stabilization and degradation. Recent studies have suggested that alterations in the expression or function of HSPC111 may be linked to pathological conditions such as cancer, neurodegenerative diseases, and autoimmune disorders. Therefore, understanding the functional mechanisms of HSPC111 at a molecular level is essential for uncovering its role in health and disease. Additionally, the development of recombinant HSPC111 proteins for experimental purposes holds promise for therapeutic innovations, including the design of targeted treatments and vaccine development. The ongoing research into HSPC111 aims to elucidate its structure-function relationships, regulatory mechanisms, and potential as a biomarker for disease progression, enhancing our overall knowledge of HSPs in cellular biology and their applications in medical research.

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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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