Recombinant Mouse Transient receptor potential cation channel subfamily M member 5 (Trpm5), partial

Code CSB-YP862381MO
MSDS
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Source Yeast
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Code CSB-EP862381MO
MSDS
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Source E.coli
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Code CSB-EP862381MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP862381MO
MSDS
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Source Baculovirus
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Code CSB-MP862381MO
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Trpm5
Uniprot No.
Alternative Names
Trpm5; Ltrpc5; Mtr1; Transient receptor potential cation channel subfamily M member 5; Long transient receptor potential channel 5; LTrpC-5; LTrpC5; MLSN1- and TRP-related gene 1 protein
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Voltage-modulated Ca(2+)-activated, monovalent cation channel (VCAM) that mediates a transient membrane depolarization and plays a central role in taste transduction. Monovalent-specific, non-selective cation channel that mediates the transport of Na(+), K(+) and Cs(+) ions equally well. Activated directly by increases in intracellular Ca(2+), but is impermeable to it. Gating is voltage-dependent and displays rapid activation and deactivation kinetics upon channel stimulation even during sustained elevations in Ca(2+). Also activated by a fast intracellular Ca(2+) increase in response to inositol 1,4,5-triphosphate-producing receptor agonists. The channel is blocked by extracellular acidification. External acidification has 2 effects, a fast reversible block of the current and a slower irreversible enhancement of current inactivation. Is a highly temperature-sensitive, heat activated channel showing a steep increase of inward currents at temperatures between 15 and 35 degrees Celsius. Heat activation is due to a shift of the voltage-dependent activation curve to negative potentials. Activated by arachidonic acid in vitro. May be involved in perception of bitter, sweet and umami tastes. May also be involved in sensing semiochemicals.
Gene References into Functions
  1. Both TRPM4 and TRPM5 are required for normal responses to bitter, sweet, and umami stimuli. PMID: 29311301
  2. This physiological and behavioral results indicate that TRPM5-MCs play a protective role in maintaining the olfactory function of the mammalian main olfactory epithelium. PMID: 28612045
  3. conclude that nAChR subunits are expressed in Trpm5-positive TRCs and their expression levels are differentially altered by chronic oral exposure to nicotine and ethanol PMID: 29293602
  4. propose that Skn-1a/Pou2f3 is the master regulator for the generation of the Trpm5-expressing microvillous cells in multiple tissues PMID: 29216297
  5. This study demonstrate that Trpm5 is transiently expressed in a subpopulation of mature OSNs in the embryonic olfactory epithelium, indicating that Trpm5 channels could play a specific role in utero during a narrow developmental time window. PMID: 28188885
  6. The PKC-dependent effect of GLP-1 on membrane potential and electrical activity was mediated by activation of Na(+)-permeable TRPM4 and TRPM5 channels by mobilization of intracellular Ca(2+) from thapsigargin-sensitive Ca(2+) stores PMID: 26571400
  7. The present findings confirm and extend our recent findings that Trpm5 KO mice express significant preferences for 8% glucose and galactose. PMID: 25497884
  8. Skn-1a is expressed in a minority of Mash1-positive olfactory progenitor cells and a majority of Trpm5-expressing microvillous cells in the main olfactory epithelium. PMID: 24428937
  9. The Trpm5 (but not T1r3) signaling is essential for starch preference, Trpm5 KO mice can learn to prefer starch based on its postoral effects. PMID: 23547138
  10. This study show that olfactory sensory neurons expressing TRPM5 respond to pheromones, but not to regular odors through the opening of CNG channels leading to Ca2+ gating of TRPM5 PMID: 24573286
  11. Evidence suggests that TRPM5 plays a role in mediating transduction for putative pheromones under conditions of reduced chemosensory input. PMID: 23613997
  12. The results suggest that pharmacological or genetic alteration of TRPM5 activity modulates the benzamil-insensitive NaCl chorda tympani response and its modulation by TRPV1 agonists. PMID: 23639808
  13. The findings of this study indicated that T1r3 and Trpm5 play critical roles in carbohydrate-induced dietary obesity. PMID: 22683548
  14. There may be a TRPM5-independent transduction pathway for detecting the taste of sweetening substances. PMID: 21987728
  15. some amygdalopetal mitral cells extended dendrites to non-TRPM5-GFP glomeruli and vice versa, suggesting that, although significant overlapping glomerular innervation is observed between these two features, it is not absolute PMID: 22120520
  16. The prototypical long-chain free fatty acid stimulus, linoleic acid, depolarizes tumor cells in vitro via activation of TRPM5. PMID: 21998136
  17. FXYD6, a Na,K-ATPase regulator, is expressed in type II taste cells. Fxyd6 is coexpressed with transient receptor potential cation channel, subfamily M, member 5 (Trpm5), a critical component of the taste signal transduction pathways. PMID: 21670532
  18. Together, these studies show that TRPM5 channels play an essential role in fatty acid transduction in mouse taste cells PMID: 21653867
  19. discussion of data from various lines of investigation on the role of TRPM4 and TRPM5 in glucose-stimulated insulin secretion in pancreatic islets PMID: 21099334
  20. membrane voltage initiated by TRPM5 channels is required for ATP secretion during taste reception PMID: 20498227
  21. Results describe a major role for TRPM5 in glucose-induced insulin secretion beyond membrane depolarization. PMID: 20393858
  22. TRPM5, a Ca(2+)-activated monovalent cation channel, is a positive regulator of glucose-induced insulin release. PMID: 20194741
  23. functions as a cationic channel that is gated when internal calcium stores are depleted and may be responsible for capacitative calcium entry in taste receptor cells that respond to bitter and/or sweet compounds. PMID: 12368808
  24. regulation of TRPM5 by Ca2+ mediates sensory activation in the taste system PMID: 14657398
  25. TRPM5 activated at lower Ca2+ concentration than TRPM4 when [Ca2+]i was raised. Different Ca2+ concentrations gave a difference in Ca2+ sensitivity between TRPM4 and TRPM5, with EC50 values of 20.2+/-4.0 microM & 0.70+/-0.1 microM, respectively. PMID: 15670874
  26. data show that extracellular acidification acts through specific residues on transient receptor potential cation channel, subfamily M(TRPM5) to block conduction through two distinct but related mechanisms PMID: 15731110
  27. TRPM5 is a highly temperature-sensitive, heat-activated channel: inward TRPM5 currents increase steeply at temperatures between 15 and 35 degrees C PMID: 16355226
  28. mouse TRPM5 gene encodes a protein of 1,158 amino acids that is proposed to have six transmembrane domains and to function as a tetramer--{REVIEW} PMID: 17217064
  29. TRPM5-expressing olfactory sensory neurons that project axons to glomeruli in the ventral area of the main olfactory bulb are involved in processing of information from semiochemicals PMID: 17267604
  30. Association between taste perception and alcohol intake, we used three different mutant mice, each lacking a gene expressed in taste buds and critical to taste transduction: alpha-gustducin (Gnat3), Tas1r3 or Trpm5. PMID: 17376151
  31. In addition to transduction channels encoded by the TRPM5 gene, taste cells have a second type of calcium activated cation channel less sensitive to intracellular calcium. PMID: 17522321
  32. We consider TRPM5 to be an intrinsic signaling component of mammalian chemosensory organs, and provide evidence for brush cells being an important cellular correlate in the periphery. PMID: 17610722
  33. This study investigated the role of these signaling proteins in the preference for fat, starch, and starch-derived polysaccharides, using Trpm5 knockout and alpha-gustducin knockout mice. PMID: 17652359
  34. that IP3R3 is a principal mediator of sweet, bitter, and umami taste perception and would be a missing molecule linking phospholipase C beta2 to TRPM5 activation. PMID: 17925404
  35. inhibition of TRPM5 by bitter compounds constitutes the molecular basis of a novel mechanism of taste interactions, whereby the bitter tastant inhibits directly the sweet transduction pathway. PMID: 18070821
  36. the TRPM5-expressing cells respond to a variety of chemicals at high exposure levels typical of irritants and are positioned in the nasal cavity appropriately to monitor inhaled air quality. PMID: 18160424
  37. that trpm5-/- mice, which lack the cellular machinery required for sweet taste transduction, can develop a robust preference for sucrose solutions based solely on caloric content. PMID: 18367093
  38. Active pharmaceutical ingredients were identified for which EC50s were essentially identical in both mouse strains, indicating a TRPM5-independent alternative aversive pathway. PMID: 18797244
  39. We provide morphological and immunocytochemical characterization of the TRPM5-expressing microvillous cells in the main olfactory epithelium PMID: 19025635
  40. Report the existence of multiple transduction pathways underlying responses to sugars: a TRPM5-independent gurmarin temperature sensitive pathway for glucose. PMID: 19211717
  41. Sensory attributes of complex tasting divalent salts are mediated by TRPM5 in mice. PMID: 19244541
  42. Solitary chemosensory cells are likely to secrete the bioactive peptides into the intestinal lumen in response to dietary factors; release of the opioid peptides requires the Trpm5 ion channel. PMID: 19272386
  43. Essential sensory transduction component from taste GPCRs for sweet, bitter, umami tastes PMID: 12581520

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Subcellular Location
Cell membrane; Multi-pass membrane protein.
Protein Families
Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM5 sub-subfamily
Tissue Specificity
Strongly expressed in liver, heart, testis, brain and kidney. Detected in fetal liver, kidney, spleen, brain, heart and lung, and in adult skin, eyes, spleen, stomach, small intestine, colon, lung, bladder, pancreas and thymus. Biallelically expressed at
Database Links
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