Cat: IPD-X40575

Recombinant Human PRR11 Protein ,His & SUMO

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Analytical Data

  • Gene name

    PRR11

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    FLJ11029 ; Homo sapiens proline rich 11 ; Proline rich protein 11 ; Proline-rich protein 11; PRR 11; Prr11; PRR11_HUMAN; transcription repressor of MHCII

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96HE9

  • Expression Region

    1-360aa

  • Molecular Weight

    56.1 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.

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Protein Description

PRR11, or Pattern Recognition Receptor 11, is a protein that plays a significant role in the immune response and has garnered attention in recent years due to its potential implications in various diseases, including cancer and autoimmune disorders. The study of PRR11 as a recombinant protein aims to elucidate its structure, function, and interactions within biological systems. Research indicates that PRR11 may be involved in recognizing specific pathogen-associated molecular patterns (PAMPs), thus activating immune signaling pathways that are essential for mounting an effective immune response. The recombinant expression of PRR11 allows for a detailed investigation of its biological properties, including its role in immune cell activation and modulation. Moreover, understanding the mechanisms by which PRR11 interacts with other immune receptors and signaling molecules can provide insights into its potential therapeutic applications. Given the increasing interest in harnessing the immune system for therapeutic benefits, such as cancer immunotherapy, the characterization of PRR11 could pave the way for novel strategies aiming to enhance immune responses. The research surrounding PRR11 also emphasizes the importance of bioengineering and protein production techniques that can facilitate large-scale studies and the development of PRR11-based diagnostics or therapeutics. Overall, the exploration of PRR11 as a recombinant protein provides a promising avenue for advancing our understanding of the immune system and developing innovative treatment modalities for immune-related diseases.

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