关键信息
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基因名
TRPM4
- 应用
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别名
1110030C19Rik; AW047689; Calcium-activated non-selective cation channel 1; FLJ20041; hTRPM4; Long transient receptor potential channel 4; LTrpC-4
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8TD43
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表达区间
964-1019aa
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分子量
8-11kda
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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
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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.
质检流程
相关产品
背景信息
TRPM4 (Transient Receptor Potential Melastatin 4) is a calcium-activated non-selective cation channel that plays a crucial role in various physiological processes, including cellular signaling, smooth muscle contraction, and immune responses. Research on TRPM4 has gained momentum due to its significant involvement in several pathophysiological conditions, such as cardiac arrhythmias, neurological disorders, and cancer. Its unique activation mechanism and permeation properties have made it a target for drug discovery, with potential implications for therapeutic interventions. The recombinant expression of TRPM4 is vital for studying its functional properties, interactions with other proteins, and modulation by various ligands. By producing TRPM4 in heterologous systems, researchers can elucidate the channel’s functional dynamics, conductance characteristics, and pharmacological profile, which are essential for understanding its role in health and disease. This research not only advances our basic understanding of TRPM4 biology but also paves the way for the development of targeted therapies aimed at modulating TRPM4 activity in pathological conditions.
