Cat: PA2000-4899

Recombinant Human hld Protein,His

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Analytical Data

  • Gene name

    hld

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    hld;Delta-hemolysin

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0A0M1

  • Expression Region

    1-26aa

  • AA Sequence

    MAQDIISTIGDLVKWIIDTVNKFTKK

  • Molecular Weight

    18.3 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

HLD (Heparin-Like Domain) recombinant proteins have gained attention in biomedical research due to their potential applications in drug development and therapeutic interventions. The HLDs are structurally similar to heparin, a naturally occurring anticoagulant, and exhibit properties that can modulate various biological processes, including cell proliferation, angiogenesis, and inflammation. Researchers have been exploring the utility of HLDs in the context of disease modeling and therapeutic targets, particularly in cancer treatment and regenerative medicine. By leveraging recombinant DNA technology, scientists have developed methods to produce HLD proteins in host systems, allowing for the detailed study of their biochemical properties and biological activities. The ability to manipulate HLD structures and enhance their functionalities through genetic engineering has opened new avenues for creating targeted therapies that can selectively interact with specific cellular receptors. Moreover, the investigation of HLDs in various pathological states might reveal novel insights into disease mechanisms, offering potential strategies for prevention and treatment. As research continues to unfold, the therapeutic promise of HLD recombinant proteins is solidifying their position as valuable tools in modern medicine, underscored by a growing body of evidence demonstrating their efficacy in preclinical studies.

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