Analytical Data
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Gene name
Uromodulin
- Application
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Alternative Names
Uromodulin; Umod; Tamm-Horsfall urinary glycoprotein; THP
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Species
Mouse
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Source
P. pastoris
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q91X17
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Expression Region
N25-F588
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AA Sequence
NSTEARRCSECHNNATCTVDGVVTTCSCQTGFTGDGLVCEDMDECATPWTHNCSNSSCVNTPGSFKCSCQDGFRLTPELSCTDVDECSEQGLSNCHALATCVNTEGDYLCVCPEGFTGDGWYCECSPGSCEPGLDCLPQGPDGKLVCQDPCNTYETLTEYWRSTEYGVGYSCDAGLHGWYRFTGQGGVRMAETCVPVLRCNTAAPMWLNGSHPSSSEGIVSRTACAHWSDQCCRWSTEIQVKACPGGFYIYNLTAPPECNLAYCTDPSSVEGTCEECRVDEDCISDNGRWRCQCKQDSNITDVSQLEYRLECGANDIKMSLRKCQLQSLGFMNVFMYLNDRQCSGFSESDERDWMSIVTPARNGPCGTVLRRNETHATYSNTLYLANAIIIRDIIIRMNFECSYPLDMKVSLKTSLQPMVSALNISLGGTGKFTVRMALFQSPTYTQPHQGPSVMLSTEAFLYVGTMLDGGDLSRFVLLMTNCYATPSSNSTDPVKYFIIQDSCPRTEDTTIQVTENGESSQARFSVQMFRFAGNYDLVYLHCEVYLCDSTSEQCKPTCSGTRF
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Molecular Weight
62.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Uromodulin, a glycoprotein primarily produced by the renal tubular cells, is the most abundant protein found in human urine. It plays a crucial role in kidney health and function, including the regulation of sodium transport, promotion of urinary tract health, and modulation of immune responses. Abnormal levels of uromodulin have been associated with various renal diseases, such as chronic kidney disease and hypertension, making it a potential biomarker for kidney dysfunction. Additionally, recombinant uromodulin has emerged as a promising therapeutic candidate due to its protective effects on renal tissues and its ability to prevent calcium phosphate crystal formation, which is linked to kidney stone development. Research efforts have focused on the production and characterization of recombinant uromodulin to explore its functional mechanisms and therapeutic applications. Advancements in recombinant protein technology have facilitated the generation of uromodulin in host systems such as bacteria or yeast, allowing for large-scale production and detailed biochemical studies. Understanding the structure-function relationship of uromodulin at the molecular level can lead to innovative treatments for kidney-related disorders and enhance our understanding of renal physiology. Overall, the investigation of recombinant uromodulin holds potential not only for therapeutic interventions but also for elucidating the biological pathways involved in kidney function and disease.
