Cat: IPD-X38451

Recombinant Human HMMR Protein,His

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Analytical Data

  • Gene name

    HMMR

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CD168; RHAMM; IHABP; RHAMM; Intracellular hyaluronic acid-binding protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O75330

  • Expression Region

    Asn577~Lys724

  • Molecular Weight

    21kDa

  • 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

HMMR, or Hyaluronan-Mediated Motility Receptor, is a significant protein involved in various cellular processes, particularly in cell motility, proliferation, and signaling pathways. Its interaction with hyaluronic acid plays a crucial role in embryonic development, tissue repair, and tumor progression. Research has increasingly focused on HMMR due to its association with cancer metastasis and poor prognosis in various malignancies. The overexpression of HMMR has been linked to enhanced migration and invasion of cancer cells, making it a potential target for therapeutic interventions. Furthermore, HMMR's role in modulating the tumor microenvironment and influencing immune responses has garnered attention in the study of cancer immunology. The generation and characterization of recombinant HMMR proteins have become essential for understanding its functional mechanisms, interactions with other cellular components, and potential therapeutic applications. Overall, the exploration of HMMR provides valuable insights into its contributions to both normal physiological processes and pathological conditions, particularly in oncology.

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