Cat: PA2000-253DB

Recombinant Human HBb Protein,His

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Analytical Data

  • Gene name

    HBb

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HBb;Hemoglobin subunit beta

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P68871

  • Expression Region

    1-147aa

  • AA Sequence

    MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH

  • Molecular Weight

    15.9 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

Hemoglobin, a crucial protein in red blood cells, is responsible for oxygen transport in the body. The study of recombinant hemoglobin (rHb) proteins has gained significant attention due to their potential applications in various medical and technological fields. Recombinant hemoglobin can be produced using genetic engineering techniques, enabling scientists to overcome limitations associated with natural hemoglobin, such as limited supply and risks of blood transfusion. Research into rHb aims to improve its stability, oxygen affinity, and overall functionality, making it a viable alternative for blood substitutes, particularly in situations where donor blood is scarce or when patients have specific transfusion requirements. Additionally, rHb can be engineered for targeted delivery of oxygen in hypoxic tissues, offering promising avenues for treating conditions like ischemia or severe anemia. The ability to produce rHb in recombinant systems also allows for the possibility of customizing its properties for specific therapeutic applications, enhancing its usability in clinical practice. As such, the ongoing research on rHb not only contributes to advancements in transfusion medicine but also paves the way for innovative treatments in respiratory and circulatory disorders. Overall, the exploration of recombinant hemoglobin represents a significant intersection of biotechnology, medicine, and molecular biology, with the potential to revolutionize how we approach oxygen delivery and therapeutic interventions.

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