Cat: PA2000-102DB

Recombinant Human HBm Protein,His

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Analytical Data

  • Gene name

    HBm

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HBm;HBAP2;Hemoglobin subunit mu

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q6B0K9

  • Expression Region

    1-141aa

  • AA Sequence

    MLSAQERAQI AQVWDLIAGH EAQFGAELLL RLFTVYPSTK VYFPHLSACQ DATQLLSHGQ RMLAAVGAAV QHVDNLRAAL SPLADLHALV LRVDPANFPL LIQCFHVVLA SHLQDEFTVQ MQAAWDKFLT GVAVVLTEKY R

  • Molecular Weight

    15.6 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.

Quality inspection process

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Protein Description

HBm recombinant protein, derived from the hepatitis B virus (HBV), has garnered significant attention in biomedical research due to its potential applications in vaccine development and therapeutic interventions. Hepatitis B is a global health concern, affecting millions and leading to serious liver diseases, including cirrhosis and hepatocellular carcinoma. The HBV surface proteins, particularly the PreS1, PreS2, and S proteins, play a crucial role in the virus's life cycle and immune response evasion. Researchers have sought to produce HBm recombinant protein to better understand HBV pathogenesis and facilitate the development of more effective vaccines. By utilizing various expression systems, such as yeast, bacteria, or mammalian cells, scientists can generate large quantities of HBm protein for structural studies, immunological assays, and drug screening. This research not only aids in elucidating the complex interactions between the virus and the host immune system but also holds promise for enhancing therapeutic strategies against hepatitis B. Overall, the study of HBm recombinant protein is critical for advancing our understanding of HBV and improving public health outcomes related to hepatitis B infections.

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