Recombinant Mouse Uromodulin (UMOD) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04550P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Uromodulin (UMOD) Protein (His)

Beta LifeScience SKU/CAT #: BLC-04550P
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Product Overview

Description Recombinant Mouse Uromodulin (UMOD) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q91X17
Target Symbol UMOD
Synonyms Umod; Uromodulin; Tamm-Horsfall urinary glycoprotein; THP) [Cleaved into: Uromodulin; secreted form]
Species Mus musculus (Mouse)
Expression System Yeast
Tag N-6His
Target Protein Sequence NSTEARRCSECHNNATCTVDGVVTTCSCQTGFTGDGLVCEDMDECATPWTHNCSNSSCVNTPGSFKCSCQDGFRLTPELSCTDVDECSEQGLSNCHALATCVNTEGDYLCVCPEGFTGDGWYCECSPGSCEPGLDCLPQGPDGKLVCQDPCNTYETLTEYWRSTEYGVGYSCDAGLHGWYRFTGQGGVRMAETCVPVLRCNTAAPMWLNGSHPSSSEGIVSRTACAHWSDQCCRWSTEIQVKACPGGFYIYNLTAPPECNLAYCTDPSSVEGTCEECRVDEDCISDNGRWRCQCKQDSNITDVSQLEYRLECGANDIKMSLRKCQLQSLGFMNVFMYLNDRQCSGFSESDERDWMSIVTPARNGPCGTVLRRNETHATYSNTLYLANAIIIRDIIIRMNFECSYPLDMKVSLKTSLQPMVSALNISLGGTGKFTVRMALFQSPTYTQPHQGPSVMLSTEAFLYVGTMLDGGDLSRFVLLMTNCYATPSSNSTDPVKYFIIQDSCPRTEDTTIQVTENGESSQARFSVQMFRFAGNYDLVYLHCEVYLCDSTSEQCKPTCSGTRF
Expression Range 25-588aa
Protein Length Partial
Mol. Weight 64.2kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability. May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF. Facilitates neutrophil migration across renal epithelia.; In the urine, may contribute to colloid osmotic pressure, retards passage of positively charged electrolytes, prevents urinary tract infection and inhibits formation of liquid containing supersaturated salts and subsequent formation of salt crystals.
Subcellular Location [Uromodulin, secreted form]: Secreted.; Apical cell membrane; Lipid-anchor, GPI-anchor. Basolateral cell membrane; Lipid-anchor, GPI-anchor. Cell projection, cilium membrane.
Database References

KEGG: mmu:22242

STRING: 10090.ENSMUSP00000033263

UniGene: PMID: 28829050

  • this study shows that uromodulin-SlpA binding dictates Lactobacillus acidophilus uptake by intestinal epithelial M cells PMID: 28992252
  • results strongly suggest that the progressive worsening of kidney functions reflects the accumulation of the deleterious effects of the misfolded mutant THP and the compensatory responses PMID: 29145399
  • Endoplasmic reticulum stress and apoptosis are key features in a mouse model of kidney disease driven by the uromodulin p.Cys147Trp mutation. PMID: 28990932
  • Consistently, pathway enrichment analysis indicates that mutant uromodulin expression affects ER function and protein homeostasis. PMID: 28437467
  • we show that Tamm-Horsfall protein deficiency stimulates proximal epithelial activation of the Interleukin-23/Interleukin-17 axis and systemic neutrophilia. PMID: 25556169
  • AGP was more effective in limiting hepatic inflammation and maintaining perfusion than saline or HAS, in both endotoxemic and septic mice. AGP sequestration of LPS may contribute to its anti-inflammatory effects. PMID: 23941548
  • UMOD upregulates TRPV5 by decreasing caveolin-1 dependent endocytosis of TRPV5. PMID: 23466996
  • UMOD regulates sodium uptake in the thick ascending limb of the loop of Henle by modulating the effect of tumor necrosis factor-alpha on NKCC2A expression, making UMOD an important determinant of blood pressure control. PMID: 24324041
  • Genetic susceptibility link to hypertension and chronic kidney disease to uromodulin expression and uromodulin's effect on salt reabsorption in the kidney. PMID: 24185693
  • Using an ischemia-reperfusion model of murine acute kidney injury, we show that, while THP expression in thick ascending loop is downregulated at the peak of injury, it is significantly upregulated 48 h after. PMID: 23389456
  • Quercetin has the uricosuric and nephroprotective actions mediated by regulating the expression levels of renal organic ion transporters and UMOD. PMID: 21909718
  • a unifying model that underscores the role of THP as a major regulator of renal and systemic immunity. PMID: 22451664
  • Molecular and cellular effects of Tamm-Horsfall protein mutations and their rescue by chemical chaperones. PMID: 22117067
  • Deletion of the von Hippel-Lindau protein (Vhl), which mediates HIF degradation under normoxia, using Tamm-Horsfall protein (Thp)-driven Cre expression showed strong expression of HIF-1alpha in thick ascending limb. PMID: 21921145
  • THP-null mouse may have a distal tubular defect and thus mimics ileostomy patients with low urine volumes and acidic urine. PMID: 21063698
  • THGP modulation of ROMK function confers a new role of THGP on renal ion transport and may contribute to salt wasting observed in FJHN/MCKD-2/GCKD patients. PMID: 21081491
  • These data clearly demonstrate a gain-of-toxic function of uromodulin mutations providing insights into the pathogenetic mechanism of the disease. PMID: 20472742
  • Normal Tamm-Horsfall protein (THP) plays an important role in defending the urinary system against calcification. Reduced expression and/or decreased function of THP could contribute to nephrolithiasis. PMID: 20591941
  • proximal 5'-flanking sequence is sufficient to drive the kidney-specific expression of a heterologous reporter gene PMID: 11880321
  • potential THP defects, either quantitative or qualitative, could predispose the urinary bladder to bacterial infections PMID: 14665435
  • THP serves as a soluble receptor for type 1 fimbriated E. coli and helps eliminate bacteria from the urinary tract. PMID: 14871399
  • THP is a critical urinary defense factor and its deficiency could be an important contributing factor in nephrolithiasis PMID: 15327412
  • Tamm-Horsfall glycoprotein plays an important regulatory role in the kidney PMID: 15522986
  • The genes encoding pre-pro-epidermal growth factor (pre-pro-EGF) and Tamm-Horsfall protein (THP)/uromodulin were aberrantly expressed in the kidneys of COX-2 -/- mice at all stages of their development. PMID: 15741608
  • Whole urine from osteopontin, Tamm-Horsfall protein , or double-null mice all possessed a dramatically reduced ability to inhibit the adhesion of calcium oxalate monohydrate crystals to renal epithelial cells PMID: 17898038
  • Urinary uromodulin is generated by a conserved C-terminal proteolytic cleavage and retains its entire ZP domain. PMID: 18375198
  • The finding that LZP might act as a new partner of THP would provide novel insights into renal functions related to THP and LZP, such as the urothelial permeability barrier and the host defense against the adhesion of pathogens. PMID: 18830570
  • Letter: Tamm-Horsfall protein knockout mice have increased stress induced micturition. PMID: 19214995
  • Umod might act as a gain-of-toxic-function mutation PMID: 19692485
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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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