Analytical Data
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基因名
VPS4A
- Application
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别名
(Protein SKD2)(VPS4-1)(hVPS4)
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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 & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9UN37
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表达区间
1-437aa
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分子量
53.9 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
VPS4A (Vacuolar Protein Sorting 4A) is a vital protein involved in the endosomal sorting complex required for transport (ESCRT) pathway, which plays a crucial role in various cellular processes, including the degradation of membrane proteins, cellular response to stress, and the regulation of various signaling pathways. Understanding the function and mechanisms of VPS4A is essential due to its implications in diseases such as cancer, where its role in maintaining cellular homeostasis and regulating apoptosis is highlighted. Research indicates that VPS4A is involved in the membrane remodeling necessary for the budding of viruses and the biogenesis of multivesicular bodies, which are key components of exosome formation. Additionally, VPS4A has been linked to cellular responses to oxidative stress and is thought to contribute to the maintenance of proteostasis within the cell. As ongoing studies explore the structural dynamics and functional properties of VPS4A, there is a growing interest in its potential as a therapeutic target, particularly in oncological contexts where the manipulation of cellular degradation pathways could enhance treatment efficacy. Therefore, characterizing VPS4A and understanding its regulatory mechanisms at the molecular level is crucial for unraveling its contribution to cellular biology and its potential implications for innovative therapeutic strategies.
