Cat: PA1000-8751

Recombinant mouse LCN5 Protein,His

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Analytical Data

  • Gene name

    LCN5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LCN5;LCN5;Epididymal-specific lipocalin-8

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A2AJB7

  • Expression Region

    27-192aa

  • AA Sequence

    TEAAVVKDFDVNKFLGFWYEIALASKMGAYGLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTRISGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHILKHDLTCVNALQSGQI

  • Molecular Weight

    22.3kDa

  • 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

LCN5, or Lipocalin 5, is a member of the lipocalin family of proteins that play significant roles in various biological processes, including lipid transport and modulation of immune responses. Recent studies have highlighted its involvement in renal function and its potential contributions to various kidney diseases. The expression of LCN5 is notably detected in the kidney, particularly in the renal tubular cells, where it is believed to be involved in the transport and metabolism of fatty acids and other lipophilic molecules. Given its functional implications, LCN5 has garnered attention as a potential biomarker and therapeutic target for conditions like diabetic nephropathy and hypertension. Research surrounding the recombinant production of LCN5 protein has been focused on characterizing its structure and elucidating its biological activities. By using techniques such as recombinant DNA technology and various expression systems, researchers aim to produce LCN5 in sufficient quantities for in-depth biochemical analyses and functional studies. Understanding the molecular mechanisms of LCN5 may lead to novel insights into its roles in health and disease and could highlight its potential utility in clinical applications. The ongoing exploration of LCN5 and its recombinant forms thus holds promise for developing innovative strategies for the diagnosis and treatment of kidney-related disorders.

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