Analytical Data
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基因名
ATP6V0C
- Application
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别名
ATP6V0C; ATP6C; ATP6L; ATPL; V-type proton ATPase 16 kDa proteolipid subunit; V-ATPase 16 kDa proteolipid subunit; Vacuolar proton pump 16 kDa proteolipid subunit
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9Y487
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表达区间
1-155aa
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氨基酸序列
MSESKSGPEYASFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPEQIMKSIIPVVMAGIIAIYGLVVAVLIANSLNDDISLYKSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK
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分子量
42.1 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
ATP6V0C, a vital component of the vacuolar ATPase (V-ATPase) complex, plays a crucial role in the regulation of cellular pH, ion homeostasis, and organelle acidification. This multi-subunit enzyme is responsible for ATP hydrolysis coupled with the translocation of protons across cellular membranes, which is essential for various physiological processes, including protein sorting, nutrient uptake, and intracellular signaling. Dysfunction of V-ATPase, particularly involving ATP6V0C, has been implicated in several pathophysiological conditions, such as cancer progression, osteopetrosis, and neurodegenerative diseases. Consequently, the study of ATP6V0C recombinant protein has garnered significant interest aimed at elucidating its structural and functional properties. Researchers are focused on characterizing its biochemical activity and exploring potential therapeutic targets that may arise from modulating V-ATPase activity. Furthermore, generating ATP6V0C recombinant proteins facilitates investigations into the assembly and regulation of the V-ATPase complex and provides a foundation for developing drugs that can target specific isoforms associated with disease states. Overall, understanding ATP6V0C not only advances our knowledge of cellular mechanisms but also opens new avenues for innovative therapeutic strategies against various health disorders.
