Cat: PA1000-7836

Recombinant Human HRNR Protein,His

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Analytical Data

  • Gene name

    HRNR

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HRNR;S100A18;Hornerin

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q86YZ3

  • Expression Region

    全长

  • AA Sequence

    full

  • 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

HRNR (horned glycoprotein) is a crucial protein involved in various biological processes, particularly in the context of skin biology and keratinocyte function. It plays a significant role in the skin barrier formation and maintenance, contributing to the prevention of water loss and protection against environmental insults. Studies have shown that HRNR is upregulated in response to injury, suggesting its involvement in wound healing and tissue repair mechanisms. The protein’s unique structure, characterized by a high content of proline and glycine, facilitates its interaction with other extracellular matrix components, highlighting its importance in cell adhesion and signaling. Given its potential therapeutic applications, researchers have focused on the recombinant expression of HRNR to produce large quantities of the protein for further functional studies and drug development. By engineering HRNR as a recombinant protein, scientists aim to elucidate its precise mechanisms of action and explore its potential in clinical settings, particularly in dermatological therapies. This research not only enhances our understanding of HRNR’s biological significance but also paves the way for innovative treatments for skin-related disorders.

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