Cat: PAX2000-12446

Recombinant Human UVRAG Protein,His

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Analytical Data

  • Gene name

    UVRAG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Beclin 1 binding Protein; DHTX; Disrupted in heterotaxy; p63; UV radiation resistance associated; UV radiation resistance associated gene; UV radiation resistance associated gene Protein; UV radiation resistance-associated gene Protein; UVRAG; UVRAG_HUMAN; VPS38

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9P2Y5

  • Expression Region

    1-699 aa

  • AA Sequence

    MSASASVGGP VPQPPPGPAA ALPPGSAARA LHVELPSQQR RLRHLRNIAA RNIVNRNGHQ LLDTYFTLHL CSTEKIYKEF YRSEVIKNSL NPTWRSLDFG IMPDRLDTSV SCFVVKIWGG KENIYQLLIE WKVCLDGLKY LGQQIHARNQ NEIIFGLNDG YYGAPFEHKG YSNAQKTILL QVDQNCVRNS YDVFSLLRLH RAQCAIKQTQ VTVQKIGKEI EEKLRLTSTS NELKKKSECL QLKILVLQNE LERQKKALGR EVALLHKQQI ALQDKGSAFS AEHLKLQLQK ESLNELRKEC TAKRELFLKT NAQLTIRCRQ LLSELSYIYP IDLNEHKDYF VCGVKLPNSE DFQAKDDGSI AVALGYTAHL VSMISFFLQV PLRYPIIHKG SRSTIKDNIN DKLTEKEREF PLYPKGGEKL QFDYGVYLLN KNIAQLRYQH GLGTPDLRQT LPNLKNFMEH GLMVRCDRHH TSSAIPVPKR QSSIFGGADV GFSGGIPSPD KGHRKRASSE NERLQYKTPP PSYNSALAQP VTTVPSMGET ERKITSLSSS LDTSLDFSKE NKKKGEDLVG SLNGGHANVH PSQEQGEALS GHRATVNGTL LPSEQAGSAS VQLPGEFHPV SEAELCCTVE QAEEIIGLEA TGFASGDQLE AFNCIPVDSA VAVECDEQVL GEFEEFSRRI YALNENVSSF RRPRRSSDK

  • Molecular Weight

    78.1 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

UVRAG (UV Radiation Resistance Associated Gene) is a critical protein that plays a pivotal role in various cellular processes, including autophagy, DNA repair, and the response to oxidative stress. Originally identified for its involvement in tumor suppression and its association with certain types of cancers, UVRAG has garnered significant interest in the scientific community for its potential therapeutic implications. Research has shown that UVRAG facilitates the maturation of autophagosomes and influences the trafficking of key proteins involved in cellular homeostasis. Given its essential functions, mutations or dysregulation of UVRAG can lead to impaired cellular responses to stress, contributing to oncogenesis and other diseases. Thus, the production of UVRAG recombinant proteins has become a focal point for investigations aimed at understanding its molecular mechanisms and interactions. By utilizing various expression systems, researchers aim to produce abundant and functional UVRAG proteins, which can then be used for structural studies, binding assays, and functional analyses. These studies are critical for elucidating the role of UVRAG in health and disease, ultimately paving the way for novel therapeutic strategies targeting UVRAG-related pathways. Furthermore, the insights gained from UVRAG research may lead to enhanced understanding of autophagy's role in cancer therapy, presenting opportunities to improve treatment efficacy through targeted approaches.

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