Cat: IPD-X38300

Recombinant Human Ab1-40 Protein,His & SUMO

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Analytical Data

  • Gene name

    Ab1-40

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Human

  • Source

    E. coli

  • Tag

    Two N- s, His- & SUMO-

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P05067

  • Expression Region

    Asp672~Val711

  • Molecular Weight

    21kDa

  • 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

Research on the Ab1-40 recombinant protein is pivotal in understanding Alzheimer's disease, a neurodegenerative disorder characterized by cognitive decline and memory loss. Ab1-40, a peptide derived from the amyloid precursor protein (APP), plays a significant role in the formation of amyloid plaques, which are hallmark features of the disease. The aggregation of Ab1-40 peptides into oligomers and fibrils is thought to contribute to neurotoxicity and synaptic dysfunction. Recombinant techniques allow for the production of highly pure Ab1-40 peptides, facilitating detailed studies on their structural properties, aggregation kinetics, and interactions with neuronal cells. Investigating the mechanisms underlying Ab1-40 pathology can aid in identifying potential therapeutic targets and biomarkers for Alzheimer's disease. Furthermore, understanding the role of post-translational modifications and mutations in the Ab1-40 sequence could provide insights into the disease's variability and progression. Overall, the study of Ab1-40 recombinant protein is essential for unraveling the complexities of Alzheimer's disease and developing effective treatments.

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