Analytical Data
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基因名
ATP6V1C1
- Application
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别名
ATP6C; ATP6D; ATP6V1C1; ATPase H+ transporting lysosomal (vacuolar proton pump) 42kD
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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
P21283
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表达区间
2-382aa
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氨基酸序列
TEFWLISAP GEKTCQQTWE KLHAATSKNN NLAVTSKFNI PDLKVGTLDV LVGLSDELAK LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLANGVDLVT YITRFQWDMA KYPIKQSLKN ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL QNLERKNAGS LLTRSLAEIV KKDDFVLDSE YLVTLLVVVP KLNHNDWIKQ YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK ARENKFIVRD FQYNEEEMKA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHVKAL RVFVESVLRY GLPVNFQAML LQPNKKTLKK LREVLHELYK HLDSSAAAII DAPMDIPGLN LSQQEYYPYV YYKIDCNLLE FK
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分子量
43.9 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
ATP6V1C1, a subunit of the V-ATPase (vacuolar-type H+-ATPase), is crucial for the acidification of intracellular organelles and plays a vital role in various cellular processes such as protein sorting, enzyme activation, and ion homeostasis. Research has shown that alterations in ATP6V1C1 expression and function are associated with several pathological conditions, including cancer, neurodegenerative diseases, and metabolic disorders. Its importance in facilitating the proton transport that maintains the pH balance within organelles has sparked interest in understanding its structure and function at the molecular level. Given its potential as a therapeutic target, studies have sought to produce and characterize recombinant ATP6V1C1 to elucidate its role in cellular physiology and disease mechanisms. The development of recombinant proteins offers a platform for investigating the biochemical properties and interactions of ATP6V1C1, paving the way for future research into its regulatory mechanisms and potential implications in targeted therapies. This research could lead to novel insights into the therapeutic modulation of V-ATPase activity in various diseases, thereby highlighting ATP6V1C1 as a significant target for drug development.
