Analytical Data
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Gene name
TRPM8
- Application
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Alternative Names
TRPM8；LTRPC6；TRPP8；Transient receptor potential cation channel subfamily M member 8
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7Z2W7
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Expression Region
690-1104aa
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AA Sequence
TKNWKIILCLFIIPLVGCGFVSFRKKPVDKHKKLLWYYVAFFTSPFVVFSWNVVFYIAFLLLFAYVLLMDFHSVPHPPELVLYSLVFVLFCDEVRQWYVNGVNYFTDLWNVMDTLGLFYFIAGIVFRLHSSNKSSLYSGRVIFCLDYIIFTLRLIHIFTVSRNLGPKIIMLQRMLIDVFFFLFLFAVWMVAFGVARQGILRQNEQRWRWIFRSVIYEPYLAMFGQVPSDVDGTTYDFAHCTFTGNESKPLCVELDEHNLPRFPEWITIPLVCIYMLSTNILLVNLLVAMFGYTVGTVQENNDQVWKFQRYFLVQEYCSRLNIPFPFIVFAYFYMVVKKCFKCCCKEKNMESSVCCFKNEDNETLAWEGVMKENYLVKINTKANDTSEEMRHRFRQLDTKLNDLKGLLKEIANKIK
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Molecular Weight
50.5 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
Related Products
Protein Description
TRPM8, a member of the transient receptor potential (TRP) ion channel family, is primarily known for its role as a cold and menthol sensor in sensory neurons. This ion channel is crucial for thermosensation and nociception, contributing to our perception of temperature and pain caused by cold stimuli. Research into TRPM8 has gained momentum due to its implications in various physiological processes, including the regulation of body temperature, pain modulation, and potentially in cancer biology. The recombinant expression of TRPM8 protein allows scientists to study its biophysical properties, ion conductance mechanisms, and molecular interactions in detail. By utilizing expression systems such as HEK293 or Sf9 cells, researchers can produce functional TRPM8 channels for electrophysiological assays, high-throughput screening, and structural studies. Investigating TRPM8 at the molecular level not only enhances our understanding of sensory transduction but also uncovers its potential as a therapeutic target for treating conditions related to pain and temperature dysregulation. As studies in this area continue to evolve, the characterization of recombinant TRPM8 proteins becomes vital for developing novel analgesic drugs and understanding the complexities of sensory physiology.
