Cat: IPD-X30946

Recombinant Mouse CAPN1 Protein,His

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Analytical Data

  • Gene name

    CAPN1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PIG30; CANPL1; MuCANP; MuCL; Calpain 1, Large Subunit; Calpain-1 Catalytic Subunit; Calcium-Dependent Protease 1; Calcium-activated neutral proteinase 1; Calpain mu-type; Micromolar-calpain

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    O35350

  • Expression Region

    Glu185~Asp356

  • Molecular Weight

    20kDa

  • 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

CAPN1, or calpain-1, is a calcium-dependent cysteine protease that plays a crucial role in various cellular processes, including cell signaling, apoptosis, and cytoskeletal remodeling. Dysregulation of CAPN1 has been implicated in several pathological conditions, including neurodegenerative diseases, cardiovascular disorders, and cancer. The study of CAPN1 and its functions has garnered increasing interest due to its potential as a therapeutic target. Recombinant CAPN1 protein production allows for detailed biochemical studies and structural analyses, facilitating the understanding of its enzymatic mechanisms and interactions with substrates. By utilizing techniques such as molecular cloning and expression systems, researchers can generate large quantities of this enzyme, enabling in vitro assays to explore its role in cellular pathways and disease mechanisms. Furthermore, recombinant CAPN1 can be employed in drug screening assays to identify small molecules that modulate its activity, thereby offering insights into novel treatment strategies for related diseases. Overall, the study of CAPN1 through recombinant protein techniques is pivotal, not only for elucidating its biological functions but also for advancing therapeutic interventions targeting calpain-related pathways.

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