Cat: IPD-X38447

Recombinant Human PLB Protein,His

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Analytical Data

  • Gene name

    PLB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PLB; PL-B1; PLB1; PLB/LIP; Phospholipase B1, membrane-associated; Phospholipase B/lipase; Lysophospholipase; Phospholipase A2

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q6P1J6

  • Expression Region

    Met1036~Leu1458

  • Molecular Weight

    51kDa

  • 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

PLB (phospholamban) is a pivotal regulatory protein found in cardiac muscle cells, playing a crucial role in calcium handling and heart function. Research into PLB is driven by its significant impact on cardiac contractility and rhythm, making it a target for understanding various cardiovascular diseases, including heart failure and arrhythmias. PLB exerts its effects by inhibiting the sarcoplasmic reticulum Ca²⁺ ATPase (SERCA), which is essential for calcium reuptake into the sarcoplasmic reticulum during relaxation of the heart muscle. This inhibitory action is modulated by the phosphorylation state of PLB, highlighting its importance in the physiological response to adrenergic stimuli. Mutations in the PLB gene have been linked to cardiomyopathies, underscoring its role in maintaining normal cardiac function. The study of PLB has expanded to encompass diverse research areas, including mechanical and molecular biology approaches to understand its structure-function relationships, modulation through phosphorylation, and potential therapeutic interventions. By exploring PLB's regulatory mechanisms, researchers aim to develop strategies to enhance cardiac performance or mitigate the effects of heart disease, making it an essential focus in cardiovascular research.

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