Cat: PAX2000-12303

Recombinant Human U2AF1L2 Protein,His

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Analytical Data

  • Gene name

    U2AF1L2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CCCH type zinc finger; CCCH type zinc finger; RNA binding motif and serine/arginine rich Protein 2; MGC142014; MGC142040; Renal carcinoma antigen NY REN 20 ; Renal carcinoma antigen NY-REN-20; RNA-binding motif and serine/arginine rich Protein 2; U2 small nuclear ribonucleoProtein auxiliary factor 35 kDa subunit related Protein 2; U2 small nuclear ribonucleoProtein auxiliary factor 35 kDa subunit-related Protein 2; U2(RNU2) small nuclear RNA auxiliary factor 1 like 2; U2(RNU2) small nuclear RNA auxiliary factor 1-like 2; U2AF1 RS2; U2AF1L2; U2AF1RS2; U2AF35-related Protein; U2AFM_HUMAN; URP; Zinc finger-; CCCH domain-; and RNA-binding motif-containing serine/arginine-rich Protein 2; Zrsr2

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q15696

  • Expression Region

    1-482 aa

  • AA Sequence

    MAAPEKMTFP EKPSHKKYRA ALKKEKRKKR RQELARLRDS GLSQKEEEED TFIEEQQLEE EKLLERERQR LHEEWLLREQ KAQEEFRIKK EKEEAAKKRQ EEQERKLKEQ WEEQQRKERE EEEQKRQEKK EKEEALQKML DQAENELENG TTWQNPEPPV DFRVMEKDRA NCPFYSKTGA CRFGDRCSRK HNFPTSSPTL LIKSMFTTFG MEQCRRDDYD PDASLEYSEE ETYQQFLDFY EDVLPEFKNV GKVIQFKVSC NLEPHLRGNV YVQYQSEEEC QAALSLFNGR WYAGRQLQCE FCPVTRWKMA ICGLFEIQQC PRGKHCNFLH VFRNPNNEFW EANRDIYLSP DRTGSSFGKN SERRERMGHH DDYYSRLRGR RNPSPDHSYK RNGESERKSS RHRGKKSHKR TSKSRERHNS RSRGRNRDRS RDRSRGRGSR SRSRSRSRRS RRSRSQSSSR SRSRGRRRSG NRDRTVQSPK SK

  • Molecular Weight

    58.0  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

U2AF1L2, a splicing factor, plays a crucial role in the regulation of RNA splicing, influencing gene expression and cellular functions. As a member of the U2AF (U2 small nuclear ribonucleic acid auxiliary factor) protein family, U2AF1L2 is involved in recognizing and binding to pre-mRNA, facilitating the assembly of the spliceosome and thereby impacting the maturation of messenger RNA transcripts. Recent studies have highlighted its significance in various biological processes and its potential links to several diseases, including cancers and hereditary disorders. Given the growing understanding of alternative splicing and its implications in disease mechanisms, the exploration of U2AF1L2's functions and interactions has become increasingly important. Researchers aim to unravel the specific roles of U2AF1L2 in cellular pathways, its interaction with other splicing factors, and how mutations or dysregulation may contribute to pathological conditions. Understanding the molecular mechanisms underlying U2AF1L2's function may provide valuable insights into therapeutic targets and strategies for diseases associated with splicing abnormalities, thereby advancing the field of molecular biology and translational medicine.

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