Cat: PAX2000-11116

Recombinant Human SAMD11 Protein,His

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Analytical Data

  • Gene name

    SAMD11

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SAMD11; Sterile alpha motif domain-containing protein 11; SAM domain-containing protein 11

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96NU1

  • Expression Region

    1-681 aa

  • AA Sequence

    MSKGILQVHP PICDCPGCRI SSPVNRGRLA DKRTVALPAA RNLKKERTPS FSASDGDSDG SGPTCGRRPG LKQEDGPHIR IMKRRVHTHW DVNISFREAS CSQDGNLPTL ISSVHRSRHL VMPEHQSRCE FQRGSLEIGL RPAGDLLGKR LGRSPRISSD CFSEKRARSE SPQEALLLPR ELGPSMAPED HYRRLVSALS EASTFEDPQR LYHLGLPSHG EDPPWHDPPH HLPSHDLLRV RQEVAAAALR GPSGLEAHLP SSTAGQRRKQ GLAQHREGAA PAAAPSFSER ELPQPPPLLS PQNAPHVALG PHLRPPFLGV PSALCQTPGY GFLPPAQAEM FAWQQELLRK QNLARLELPA DLLRQKELES ARPQLLAPET ALRPNDGAEE LQRRGALLVL NHGAAPLLAL PPQGPPGSGP PTPSRDSARR APRKGGPGPA SARPSESKEM TGARLWAQDG SEDEPPKDSD GEDPETAAVG CRGPTPGQAP AGGAGAEGKG LFPGSTLPLG FPYAVSPYFH TGAVGGLSMD GEEAPAPEDV TKWTVDDVCS FVGGLSGCGE YTRVFREQGI DGETLPLLTE EHLLTNMGLK LGPALKIRAQ VARRLGRVFY VASFPVALPL QPPTLRAPER ELGTGEQPLS PTTATSPYGG GHALAGQTSP KQENGTLALL PGAPDPSQPL C

  • Molecular Weight

    72.7 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

The SAMD11 protein, belonging to the SAM (Sterile Alpha Motif) domain-containing protein family, has garnered significant attention in recent years due to its potential roles in cellular processes and disease mechanisms. Research has increasingly indicated that SAMD11 is involved in various biological functions, including cell differentiation, immune response, and the regulation of gene expression. Given its structural features, SAMD11 is hypothesized to participate in protein-protein interactions, which are crucial for many cellular signaling pathways. Furthermore, studies suggest that alterations in SAMD11 expression may be linked to various pathological conditions, including cancer and autoimmune disorders. The generation of recombinant SAMD11 protein is essential for elucidating its functional roles and interactions within the cell, as it allows for the examination of its biochemical properties in controlled experimental settings. This recombinant protein can be used in assays to study its binding affinities and functional dynamics, aiding in the identification of potential therapeutic targets. Therefore, understanding the biology of SAMD11 not only advances our knowledge of fundamental cellular processes but also holds promise for the development of novel strategies in disease intervention and treatment. Research efforts focusing on the characterization and functional analysis of SAMD11 are critical, as they pave the way for unraveling its contributions to health and disease.

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