Cat: PA1000-4678

Recombinant Human CST8 Protein,His

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Analytical Data

  • Gene name

    CST8

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CST8;CRES;Cystatin-8

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O60676

  • Expression Region

    22-142aa

  • AA Sequence

    KDPKKNETG VLRKLKPVNA SNANVKQCLW FAMQEYNKES EDKYVFLVVK TLQAQLQVTN LLEYLIDVEI ARSDCRKPLS TNEICAIQEN SKLKRKLSCS FLVGALPWNG EFTVMEKKCE DA

  • 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

CST8, also known as cystatin F, is a member of the cystatin superfamily of cysteine protease inhibitors. It has garnered attention in recent years due to its potential role in various physiological and pathological processes, including immunity, inflammation, and cancer progression. Research indicates that CST8 may interact with enzymes within the cysteine protease family, modulating their activity and influencing immune cell function. Studies have shown that altered expression of CST8 can affect the tumor microenvironment and may contribute to tumorigenesis. Consequently, understanding the structure and function of CST8, particularly focusing on recombinant protein production, is critical for elucidating its biological roles. By employing recombinant DNA technology to produce CST8, researchers can investigate its biochemical properties, functional mechanisms, and potential applications in therapeutic interventions. This line of research holds promise for developing innovative strategies for treating diseases where CST8 is implicated, as well as providing insights into the intricate regulatory networks governing immune response and cancer biology.

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