Cat: IPD-X39840

Recombinant Larimichthys crocea hamp Protein

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Analytical Data

  • Gene name

    hamp

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    hamp; Hepcidin

  • Species

    Larimichthys crocea

  • Source

    E. coli

  • Tag

    Tag Free

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A1Z0M0

  • Expression Region

    65-85aa

  • Molecular Weight

    2.5 kDa

  • 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

HAMP (Hepcidin Antimicrobial Peptide) is a vital regulator of iron homeostasis and plays a crucial role in the body's response to inflammation and infection. Initially discovered for its antimicrobial properties, HAMP regulates systemic iron levels by controlling the absorption of dietary iron and the release of iron from macrophages and liver cells. Dysregulation of HAMP is implicated in various disorders, such as anemia of chronic disease, hereditary hemochromatosis, and iron overload syndromes. Understanding the structure and function of HAMP is essential for developing potential therapeutic strategies targeting these conditions. Recent research has focused on the recombinant production of HAMP to study its functional mechanisms, structure-function relationships, and interactions with iron transport proteins and receptors. This has enabled scientists to explore the peptide's role not only in iron metabolism but also in various pathophysiological processes, including inflammation and infection. The ongoing investigation into HAMP and its recombinant forms aims to enhance our understanding of iron regulation and develop innovative treatments for related disorders, thereby addressing a significant clinical challenge associated with iron management in diseases.

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