Cat: PAX2000-12166

Recombinant Human TRIM49 Protein,His

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Analytical Data

  • Gene name

    TRIM49

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RING finger Protein 18; RNF 18; RNF18; Testis specific RING Finger Protein; Testis-specific ring-finger Protein; TRI49_HUMAN; TRIM 49; TRIM49; Tripartite motif containing 49; Tripartite motif containing Protein 49; Tripartite motif-containing Protein 49

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0CI25

  • Expression Region

    1-452 aa

  • AA Sequence

    MNSGILQVFQ GELICPLCMN YFIDPVTIDC GHSFCRPCFY LNWQDIPFLV QCSECTKSTE QINLKTNIHL KKMASLARKV SLWLFLSSEE QMCGTHRETK KIFCEVDRSL LCLLCSSSQE HRYHRHRPIE WAAEEHREKL LQKMQSLWEK ACENHRNLNV ETTRTRCWKD YVNLRLEAIR AEYQKMPAFH HEEEKHNLEM LKKKGKEIFH RLHLSKAKMA HRMEILRGMY EELNEMCHKP DVELLQAFGD ILHRSESVLL HMPQPLNPEL SAGPITGLRD RLNQFRVHIT LHHEEANNDI FLYEILRSMC IGCDHQDVPY FTATPRSFLA WGVQTFTSGK YYWEVHVGDS WNWAFGVCNM YRKEKNQNEK IDGKAGLFLL GCVKNDIQCS LFTTSPLMLQ YIPKPTSRVG LFLDCEAKTV SFVDVNQSSL IYTIPNCSFS PPLRPIFCCI HF

  • Molecular Weight

    52.8 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

TRIM49 (tripartite motif-containing protein 49) is a member of the TRIM protein family, known for its roles in various biological processes, including immunity, cell proliferation, and apoptosis. The TRIM proteins share a common tripartite structure comprising a RING finger, a B-box, and a coiled-coil domain, which facilitate their E3 ubiquitin ligase activity. Recent studies have highlighted TRIM49's potential involvement in the modulation of immune responses and its role in regulating inflammatory pathways. Understanding TRIM49 function is particularly relevant in the context of infectious diseases and cancer, where it may influence the stability and activity of key signaling proteins. Research has suggested that TRIM49 could be a crucial mediator in the immune response to viral infections, as it may target viral proteins for degradation, thereby impacting viral replication. Furthermore, its dysregulation has been associated with various diseases, which underscores the importance of characterizing its activity and interactions. Investigating TRIM49 through the production of recombinant proteins allows for detailed functional analysis and the exploration of its potential as a therapeutic target. This research is vital not only for elucidating the specific mechanisms underlying TRIM49's action within the immune system but also for developing novel strategies for disease intervention based on its regulatory functions. Overall, TRIM49 presents as a promising candidate for further study in the hopes of uncovering new insights into immune regulation and potential therapeutic applications.

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