Cat: IPD-X14118

Recombinant Mouse BNP Protein, N- His & GST

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Analytical Data

  • Gene name

    BNP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    NT-Pro-BNP; ; N-BNP

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 85% as determined by SDS-PAGE.

  • Uniprot

    P40753

  • Expression Region

    Tyr27~Arg76

  • Protein Length

    Partial

  • Molecular Weight

    40kDa

  • 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

B-type Natriuretic Peptide (BNP) is a crucial biomarker historically associated with heart failure and other cardiovascular conditions, possessing significant roles in cardiovascular homeostasis and regulation of blood pressure. The peptide is released by the ventricles in response to increased cardiac wall stress, signifying heart strain and dysfunction. In recent years, the research focus has shifted towards the exploration of BNP's role as a therapeutic target and its potential in regenerative medicine. The reconfiguration of BNP into recombinant proteins aims to enhance its stability, bioavailability, and therapeutic efficacy. Advances in recombinant DNA technology have allowed for the production of BNPrelated proteins that exhibit improved pharmacokinetics and pharmacodynamics compared to native BNP. This research addresses the challenges of conventional treatments for heart failure and opens doors for innovative therapies aimed at restoring cardiac function. With the increasing prevalence of cardiovascular diseases globally, the development of engineered BNP may offer promising avenues for more effective and targeted treatment strategies, providing hope for better management of heart-related ailments and improved patient outcomes.

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