Cat: PAX2000-12184

Recombinant Human TRIM8 Protein,His

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Analytical Data

  • Gene name

    TRIM8

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    AA408830; BB006755; GERP; Glioblastoma-expressed RING finger Protein; Lioblastoma expressed ring finger Protein; Probable E3 ubiquitin-Protein ligase TRIM8; RING finger Protein 27; RNF27; RP11-47A8.4; TRIM8; TRIM8_HUMAN; Tripartite motif containing 8; Tripartite motif Protein TRIM8; Tripartite motif-containing Protein 8

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BZR9

  • Expression Region

    1-551 aa

  • AA Sequence

    MAENWKNCFE EELICPICLH VFVEPVQLPC KHNFCRGCIG EAWAKDSGLV RCPECNQAYN QKPGLEKNLK LTNIVEKFNA LHVEKPPAAL HCVFCRRGPP LPAQKVCLRC EAPCCQSHVQ THLQQPSTAR GHLLVEADDV RAWSCPQHNA YRLYHCEAEQ VAVCQYCCYY SGAHQGHSVC DVEIRRNEIR KMLMKQQDRL EEREQDIEDQ LYKLESDKRL VEEKVNQLKE EVRLQYEKLH QLLDEDLRQT VEVLDKAQAK FCSENAAQAL HLGERMQEAK KLLGSLQLLF DKTEDVSFMK NTKSVKILMD RTQTCTSSSL SPTKIGHLNS KLFLNEVAKK EKQLRKMLEG PFSTPVPFLQ SVPLYPCGVS SSGAEKRKHS TAFPEASFLE TSSGPVGGQY GAAGTASGEG QSGQPLGPCS STQHLVALPG GAQPVHSSPV FPPSQYPNGS AAQQPMLPQY GGRKILVCSV DNCYCSSVAN HGGHQPYPRS GHFPWTVPSQ EYSHPLPPTP SVPQSLPSLA VRDWLDASQQ PGHQDFYRVY GQPSTKHYVT S

  • Molecular Weight

    61.4 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

TRIM8, a member of the tripartite motif (TRIM) protein family, has garnered significant research interest due to its diverse roles in cellular processes such as immune response, cell proliferation, and apoptosis. The TRIM family is characterized by a RING domain, one or two B-box domains, and a coiled-coil region, enabling them to function as E3 ubiquitin ligases. TRIM8, in particular, is known for its involvement in regulating various signaling pathways, including those associated with viral infection and cancer. Research has indicated that TRIM8 can modulate the stability of key cellular proteins and influence inflammatory responses, making it a crucial player in the pathogenesis of numerous diseases. Recent studies have also linked TRIM8 to the modulation of the immune system, where it acts to either promote or inhibit inflammatory responses depending on the context. Moreover, its dysregulation has been associated with several pathological conditions, such as autoimmune diseases and certain cancers, underscoring its potential as a therapeutic target. Understanding the molecular mechanisms underlying TRIM8's function and its interactions may provide insights into novel strategies for disease intervention. Therefore, the study of TRIM8 recombinant protein not only aids in elucidating its biological functions but also opens avenues for developing targeted therapeutics that can exploit its role in disease modulation.

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