Cat: PA1000-8764

Recombinant Human MK Protein,His

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Analytical Data

  • Gene name

    MK

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MK;MK1;NEGF2;Midkine

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P21741

  • Expression Region

    1-143aa

  • AA Sequence

    MQHRGFLLLTLLALLALTSAVAKKKDKVKKGGPGSECAEWAWGPCTPSSKDCGVGFREGTCGAQTQRIRCRVPCNWKKEFGADCKYKFENWGACDGGTGTKVRQGTLKKARYNAQCQETIRVTKPCTPKTKAKAKAKKGKGKD

  • Molecular Weight

    15.5 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.

Quality inspection process

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Protein Description

MK (mitogen kinase) proteins are a family of serine/threonine kinases that play crucial roles in various cellular processes, including cell proliferation, differentiation, and response to stress signals. Their dysregulation has been implicated in numerous diseases, particularly cancer, where abnormal MK signaling pathways contribute to tumor growth and metastasis. Research into MK proteins has gained momentum due to their potential as therapeutic targets; inhibiting their activity may offer new avenues for cancer treatment. Furthermore, MK proteins are involved in other physiological and pathological processes, such as neurodegenerative diseases and cardiovascular disorders, underlining the need for a comprehensive understanding of their biological functions. Recent advances in molecular biology and biochemistry techniques have facilitated the identification and characterization of specific MK isoforms and their regulatory mechanisms. The development of small molecule inhibitors and monoclonal antibodies targeting MK proteins is an area of active investigation and holds promise for enhancing therapeutic efficacy while minimizing side effects. As researchers continue to unravel the complex signaling networks involving MK proteins, the potential for novel biomarker discovery and personalized medicine approaches increases, showcasing the significance of MK proteins in both fundamental biology and clinical applications.

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