Cat: IPD-X13999

Recombinant Pig Insulin Protein, N- His & GST

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Analytical Data

  • Gene name

    Insulin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Insulin; INS; IDDM; ILPR; IRDN; MODY10

  • Species

    Pig

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P01315

  • Expression Region

    Phe25~Ala54

  • Protein Length

    Partial

  • Molecular Weight

    35kDa

  • 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.

Quality inspection process

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Protein Description

Recombinant insulin, a synthetic form of human insulin produced through recombinant DNA technology, emerged as a groundbreaking advancement in diabetes management in the late 20th century. Prior to this innovation, insulin was primarily sourced from animal pancreas, which posed several challenges, including variability in potency, allergic reactions, and ethical concerns regarding animal welfare. The development of recombinant insulin addressed these issues by allowing for a more consistent and pure product that closely mimics human insulin. Research efforts focused on cloning the human insulin gene and introducing it into bacteria or yeast, making it possible to produce insulin in large quantities. Since its introduction, recombinant insulin has revolutionized the treatment of diabetes, offering patients improved glycemic control and reduced risk of complications. Further research has continued to enhance insulin analogs, leading to the creation of long-acting and rapid-acting formulations tailored to individual patient needs. Overall, the study of recombinant insulin not only highlights significant advancements in biotechnology but also underscores the ongoing commitment to innovation in healthcare for chronic disease management.

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