Analytical Data
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基因名
VAChT
- Application
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别名
VAChT；VACHT；Vesicular acetylcholine transporter
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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
Q16572
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表达区间
1-532aa
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氨基酸序列
MESAEPAGQARAAATKLSEAVGAALQEPRRQRRLVLVIVCVALLLDNMLYMVIVPIVPDYIAHMRGGGEGPTRTPEVWEPTLPLPTPANASAYTANTSASPTAAWPAGSALRPRYPTESEDVKIGVLFASKAILQLLVNPLSGPFIDRMSYDVPLLIGLGVMFASTVLFAFAEDYATLFAARSLQGLGSAFADTSGIAMIADKYPEEPERSRALGVALAFISFGSLVAPPFGGILYEFAGKRVPFLVLAAVSLFDALLLLAVAKPFSAAARARANLPVGTPIHRLMLDPYIAVVAGALTTCNIPLAFLEPTIATWMKHTMAASEWEMGMAWLPAFVPHVLGVYLTVRLAARYPHLQWLYGALGLAVIGASSCIVPACRSFAPLVVSLCGLCFGIALVDTALLPTLAFLVDVRHVSVYGSVYAIADISYSVAYALGPIVAGHIVHSLGFEQLSLGMGLANLLYAPVLLLLRNVGLLTRSRSERDVLLDEPPQGLYDAVRLRERPVSGQDGEPRSPPGPFDACEDDYNYYYTRS
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分子量
56.9 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
Vesicular acetylcholine transporter (VAChT) is a critical protein responsible for packaging the neurotransmitter acetylcholine into vesicles within cholinergic neurons, thereby playing a pivotal role in cholinergic signaling and neurotransmission. The study of VAChT is essential for understanding various physiological processes and the pathophysiology of neurodegenerative diseases, such as Alzheimer's disease, where cholinergic systems are significantly affected. Research into the structure, function, and regulation of VAChT has been supported by advances in recombinant protein technology, allowing for detailed studies of its biochemical properties and interactions with other cellular components. The expression and purification of VAChT as a recombinant protein enable researchers to investigate its functional mechanisms, explore potential pharmacological targets, and develop therapeutic strategies to enhance cholinergic function. Additionally, studying VAChT can provide insights into synaptic vesicle dynamics and the broader implications of vesicular transporters in neurotransmitter release. This research contributes not only to our fundamental understanding of neurobiology but also holds potential for developing innovative treatments for cognitive disorders.
