Cat: PA1000-8757

Recombinant Human LCNL1 Protein,His

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Analytical Data

  • Gene name

    LCNL1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LCNL1;Lipocalin-like 1 Protein

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q6ZST4

  • Expression Region

    1-164aa

  • AA Sequence

    MVGVVSDDQD FLDSKDTMKM AVVLVTPLGN GDLALKFGYP TPHGGCQKMD TTFTEGAVPG QFSNPAMALS DIRVAFSDYQ HFALLYLEMR KGGLRNQWLQ LYGGRAAGRR PRHPRFGSGM SPLCLHQPFL HAEGGTAGSW CLWPRVPAPP CPSLPLFAPP APSL

  • 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

LCNL1, or Leucine-Cysteine-rich Nuclear Protein 1, has emerged as a significant focus of research due to its implicated roles in various biological processes, particularly in cell signaling, stress response, and transcriptional regulation. Discovered through genomic studies, LCNL1's unique structural features, characterized by a high content of leucine and cysteine residues, suggest its involvement in protein-protein interactions and cellular compartmentalization. Preliminary studies have indicated that LCNL1 may be linked to certain diseases, including cancer and neurodegenerative disorders, highlighting its potential as a biomarker or therapeutic target. The recombinant expression of LCNL1 allows for detailed functional assays and structural analyses, providing insights into its molecular mechanisms. Researchers are particularly interested in understanding how LCNL1 modulates cellular pathways under physiological and pathological conditions. Overall, the study of LCNL1 recombinant protein holds promise for advancing knowledge in molecular biology, with the potential to unlock new approaches for disease diagnosis and treatment.

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