Cat: PAX2000-11216

Recombinant Human SENP5 Protein,His

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Analytical Data

  • Gene name

    SENP5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    FKSG45; FLJ42398; MGC27076; Protease FKSG45; SENP5; SENP5_HUMAN; Sentrin specific protease SENP5; Sentrin-specific protease 5; Sentrin/SUMO specific protease SENP5; Sentrin/SUMO-specific protease SENP5; SUMO specific protease SENP5; SUMO1/sentrin specific peptidase 5; SUMO1/sentrin specific protease 5

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96HI0

  • Expression Region

    1-755 aa

  • AA Sequence

    MKKQRKILWR KGIHLAFSEK WNTGFGGFKK FYFHQHLCIL KAKLGRPVTW NRQLRHFQGR KKALQIQKTW IKDEPLCAKT KFNVATQNVS TLSSKVKRKD AKHFISSSKT LLRLQAEKLL SSAKNSDHEY CREKNLLKAV TDFPSNSALG QANGHRPRTD PQPSDFPMKF NGESQSPGES GTIVVTLNNH KRKGFCYGCC QGPEHHRNGG PLIPKKFQLN QHRRIKLSPL MMYEKLSMIR FRYRILRSQH FRTKSKVCKL RKAQRSWVQK VTGDHQETRR ENGEGGSCSP FPSPEPKDPS CRHQPYFPDM DSSAVVKGTN SHVPDCHTKG SSFLGKELSL DEAFPDQQNG SATNAWDQSS CSSPKWECTE LIHDIPLPEH RSNTMFISET EREIMTLGQE NQTSSVSDDR VKLSVSGADT SVSSVDGPVS QKAVQNENSY QMEEDGSLKQ SILSSELLDH PYCKSPLEAP LVCSGLKLEN QVGGGKNSQK ASPVDDEQLS VCLSGFLDEV MKKYGSLVPL SEKEVLGRLK DVFNEDFSNR KPFINREITN YRARHQKCNF RIFYNKHMLD MDDLATLDGQ NWLNDQVINM YGELIMDAVP DKVHFFNSFF HRQLVTKGYN GVKRWTKKVD LFKKSLLLIP IHLEVHWSLI TVTLSNRIIS FYDSQGIHFK FCVENIRKYL LTEAREKNRP EFLQGWQTAV TKCIPQQKND SDCGVFVLQY CKCLALEQPF QFSQEDMPRV RKRIYKELCE CRLMD

  • Molecular Weight

    86.6 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

SENP5 (Sentrin/SUMO-specific protease 5) is a crucial enzyme involved in the SUMO (Small Ubiquitin-like Modifier) pathway, which plays a significant role in post-translational modifications that regulate various cellular processes, including protein stability, localization, and function. Research has shown that SENP5 is involved in the deconjugation of SUMO proteins from their substrates, thereby influencing critical biological functions such as gene expression, cell cycle progression, and stress responses. Abnormal SENP5 activity has been implicated in several diseases, including cancer, where it may contribute to tumorigenesis by altering the SUMOylation status of oncogenic and tumor suppressor proteins. Consequently, the study of recombinant SENP5 protein is pivotal for understanding its enzymatic mechanisms, the specificity of SUMO substrates, and the regulatory networks to which it contributes. By utilizing recombinant DNA technology, researchers can produce large quantities of purified SENP5 protein to investigate its biochemical properties, interactive partners, and the effects of specific mutations. Through these studies, SENP5 may be identified as a potential therapeutic target, offering new avenues for drug development aimed at modulating its activity for disease intervention. This growing interest underscores the importance of SENP5 in both basic and applied biomedical research, paving the way for novel insights into SUMO-mediated regulation in health and disease.

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