Cat: IPD-X14005

Recombinant Human Proinsulin Protein, N- His & GST

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Analytical Data

  • Gene name

    Proinsulin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    INS; Pro-Insulin; Preproinsulin

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 97% as determined by SDS-PAGE.

  • Uniprot

    -

  • Expression Region

    Phe25~Asn110

  • Protein Length

    Partial

  • Molecular Weight

    41kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    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.

  • Storage & Shelf Life

    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.

  • Shipping

    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

Proinsulin, the precursor of insulin, is a critical component in the regulation of glucose metabolism and is pivotal for the treatment of diabetes. The study of recombinant proinsulin has gained significance due to its potential for therapeutic applications. In the 1920s, insulin was first discovered as a treatment for diabetes, but its production was limited to animal sources until the advent of recombinant DNA technology in the 1970s. This breakthrough allowed for the production of human insulin and proinsulin using genetically modified organisms, such as bacteria and yeast, ensuring a consistent and safer source compared to animal-derived products. Research into proinsulin's structure and function has revealed its role in the formation of insulin, highlighting the importance of understanding this precursor for both basic science and clinical applications. Furthermore, proinsulin itself has generated interest for its potential use as a biomarker for early diabetes detection and as a therapeutic target. Current studies focus on enhancing methods for its production, purification, and characterization, which are essential for ongoing advancements in diabetes management. Investigating proinsulin has thus become a vital area of research, aimed at bridging the gap between basic endocrinology and the clinical treatment of diabetes, ultimately contributing to the development of novel therapies that improve patient outcomes.

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