Cat: PAX2000-11945

Recombinant Human THEA Protein,His

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Analytical Data

  • Gene name

    THEA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ACO11_HUMAN; ACOT 11; ACOT11; Acyl CoA thioester hydrolase 11; Acyl CoA thioesterase 11; Acyl coenzyme A thioesterase 11; Acyl-CoA thioester hydrolase 11; Acyl-CoA thioesterase 11; Acyl-coenzyme A thioesterase 11; Adipose associated thioesterase; Adipose-associated thioesterase; BFIT 1; BFIT 2; BFIT; BFIT1; BFIT2; Brown fat inducible thioesterase; Brown fat-inducible thioesterase; KIAA0707; OTTHUMP00000046722; StAR related lipid transfer (START) domain containing 14; STARD 14; STARD14; START domain containing 14; THEA; THEM 1; THEM1; Thioesterase adipose associated; Thioesterase superfamily member 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q8WXI4

  • Expression Region

    1-607 aa

  • AA Sequence

    MIQNVGNHLR RGLASVFSNR TSRKSALRAG NDSAMADGEG YRNPTEVQMS QLVLPCHTNQ RGELSVGQLL KWIDTTACLS AERHAGCPCV TASMDDIYFE HTISVGQVVN IKAKVNRAFN SSMEVGIQVA SEDLCSEKQW NVCKALATFV ARREITKVKL KQITPRTEEE KMEHSVAAER RRMRLVYADT IKDLLANCAI QGDLESRDCS RMVPAEKTRV ESVELVLPPH ANHQGNTFGG QIMAWMENVA TIAASRLCRA HPTLKAIEMF HFRGPSQVGD RLVLKAIVNN AFKHSMEVGV CVEAYRQEAE THRRHINSAF MTFVVLDADD QPQLLPWIRP QPGDGERRYR EASARKKIRL DRKYIVSCKQ TEVPLSVPWD PSNQVYLSYN NVSSLKMLVA KDNWVLSSEI SQVRLYTLED DKFLSFHMEM VVHVDAAQAF LLLSDLRQRP EWDKHYRSVE LVQQVDEDDA IYHVTSPALG GHTKPQDFVI LASRRKPCDN GDPYVIALRS VTLPTHRETP EYRRGETLCS GFCLWREGDQ LTKCCWVRVS LTELVSASGF YSWGLESRSK GRRSDGWNGK LAGGHLSTLK AIPVAKINSR FGYLQDT

  • Molecular Weight

    68.4 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

The study of THEA (Tetrahydroxyethylamino) recombinant proteins has gained notable interest due to their potential applications in biotechnology and medicine. Recombinant proteins are engineered proteins that are produced using recombinant DNA technology, allowing for the expression of specific proteins in host organisms, commonly bacteria, yeast, or mammalian cells. THEA proteins, characterized by their unique structural and functional properties, are believed to play pivotal roles in various biological processes, including cellular signaling, immune response, and metabolic regulation. Their ability to be tailored for improved stability and activity makes them crucial candidates for therapeutic use, such as vaccine development or enzyme replacement therapy. The exploration of THEA recombinant proteins involves extensive research aimed at understanding their molecular mechanisms, optimizing expression systems, and assessing their clinical efficacy. Moreover, advancements in protein engineering and purification techniques have further propelled the study of these proteins, opening new avenues for innovative treatments and diagnostic tools in the healthcare sector. The ongoing research endeavors underscore the significance of THEA recombinant proteins in advancing our understanding of biochemistry and developing next-generation biopharmaceuticals.

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