Analytical Data
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基因名
TRPM8
- Application
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别名
TRPM8；LTRPC6；TRPP8；Transient receptor potential cation channel subfamily M member 8
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q7Z2W7
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表达区间
690-1104aa
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氨基酸序列
TKNWKIILCLFIIPLVGCGFVSFRKKPVDKHKKLLWYYVAFFTSPFVVFSWNVVFYIAFLLLFAYVLLMDFHSVPHPPELVLYSLVFVLFCDEVRQWYVNGVNYFTDLWNVMDTLGLFYFIAGIVFRLHSSNKSSLYSGRVIFCLDYIIFTLRLIHIFTVSRNLGPKIIMLQRMLIDVFFFLFLFAVWMVAFGVARQGILRQNEQRWRWIFRSVIYEPYLAMFGQVPSDVDGTTYDFAHCTFTGNESKPLCVELDEHNLPRFPEWITIPLVCIYMLSTNILLVNLLVAMFGYTVGTVQENNDQVWKFQRYFLVQEYCSRLNIPFPFIVFAYFYMVVKKCFKCCCKEKNMESSVCCFKNEDNETLAWEGVMKENYLVKINTKANDTSEEMRHRFRQLDTKLNDLKGLLKEIANKIK
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分子量
50.5 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
