Cat: PAX2000-10795

Recombinant Human RBM15 Protein,GST

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Analytical Data

  • Gene name

    RBM15

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    One twenty two protein ; One-twenty two protein 1; OTT; OTT1; Putative RNA-binding protein 15; RBM15; RBM15_HUMAN; RNA binding motif protein 15; RNA-binding motif protein 15

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96T37

  • Expression Region

    1-563 aa

  • AA Sequence

    MPEDDQRATRNLFIGNLDHSVSEVELRRAFEKYGIIEEVVIKRPARGQGGAYAFLKFQNLDMAHRAKVAMSGRVIGRNPIKIGYGKANPTTRLWVGGLGPNTSLAALAREFDRFGSIRTIDHVKGDSFAYIQYESLDAAQAACAKMRGFPLGGPDRRLRVDFAKAEETRYPQQYQPSPLPVHYELLTDGYTRHRNLDADLVRDRTPPHLLYSDRDRTFLEGDWTSPSKSSDRRNSLEGYSRSVRSRSGERWGADGDRGLPKPWEERRKRRSLSSDRGRTTHSPYEERSRTKGSGQQSERGSDRTPERSRKENHSSEGTKESSSNSLSNSRHGAEERGHHHHHHEAADSSHGKKARDSERNHRTTEAEPKPLEEPKHETKKLKNLSEYAQTLQLGWNGLLVLKNSCFPTSMHILEGDQGVISSLLKDHTSGSKLTQLKIAQRLRLDQPKLDEVTRRIKQGSPNGYAVLLATQATPSGLGTEGMPTVEPGLQRRLLRNLVSYLKQKQAAGVISLPVGGSKGRDGTGMLYAFPPCDFSQQYLQSALRTLGKLEEEHMVIVIVRDTA

  • Molecular Weight

    88.33 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

RBM15 (RNA-binding motif protein 15) is a key regulator in various biological processes, including RNA splicing, gene expression, and cell differentiation. Research into RBM15 has gained momentum due to its significant role in hematopoiesis and its association with specific hematological malignancies. The protein is part of the splicing factor complex and is implicated in the regulation of alternative splicing events, which can impact cell fate decisions. Recent studies have highlighted the importance of RBM15 in maintaining stem cell properties and its involvement in the development of acute myeloid leukemia (AML), where it may act as an oncogenic factor. The understanding of RBM15 function is further complicated by the presence of several isoforms and the interplay with other regulatory proteins. Furthermore, the study of RBM15's role in gene expression regulation and its potential as a therapeutic target underscores the need for detailed analysis of its domain structure and interaction networks. Consequently, the generation of recombinant RBM15 protein has become a focal point of research, enabling researchers to dissect its molecular functions and explore its potential roles in disease mechanisms and novel therapeutic strategies. By investigating the biochemical properties and interactions of RBM15, researchers aim to elucidate its contributions to normal cellular processes and how its dysregulation may lead to pathologies, thereby opening new avenues for targeted therapies in cancers and other diseases where RBM15 plays a crucial role.

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