Cat: PAX2000-12144

Recombinant Human TRIM23 Protein,His

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Analytical Data

  • Gene name

    TRIM23

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ADP ribosylation factor domain Protein 1; ADP-ribosylation factor domain-containing Protein 1; ARF domain Protein 1; ARFD1; E3 ubiquitin-Protein ligase TRIM23; GTP binding Protein ARD 1; GTP-binding Protein ARD-1; N-acetyltransferase ARD1 human homolog of; N-acetyltransferase homolog of S. cerevisiae ARD1; RING finger Protein 46; TRI23_HUMAN; TRIM23; Tripartite motif Protein TRIM23; Tripartite motif-containing Protein 23

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P36406

  • Expression Region

    1-574 aa

  • AA Sequence

    MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA

  • Molecular Weight

    64.0 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

TRIM23, a member of the TRIM (tripartite motif-containing) protein family, has garnered increasing attention in recent years due to its potential roles in various cellular processes, including immune response, cell differentiation, and oncogenesis. TRIM proteins are characterized by a RING finger domain, B-box, and coiled-coil region, which facilitate their functions as E3 ubiquitin ligases, regulating protein degradation and thereby influencing cell signaling pathways. Research has shown that TRIM23 can modulate the stability of several key proteins involved in cancer progression and immune regulation. Moreover, studies suggest that TRIM23 might play a critical role in the response to viral infections by influencing the activity of interferon signaling pathways. Understanding the intricate mechanisms of TRIM23's action may provide valuable insights into its potential as a therapeutic target for cancer and viral diseases. Recent advancements in structural biology have enabled the characterization of the TRIM23 protein at the molecular level, presenting opportunities for drug design and development. Investigating TRIM23's interactions with other cellular proteins and its influence on various signaling pathways is essential for elucidating its biological significance. Ultimately, the exploration of TRIM23 could pave the way for novel interventions in treating diseases where its dysregulation is implicated.

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