Analytical Data
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Gene name
ATP6V1C1
- Application
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Alternative Names
ATP6C; ATP6D; ATP6V1C1; ATPase H+ transporting lysosomal (vacuolar proton pump) 42kD
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21283
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Expression Region
2-382aa
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AA Sequence
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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Molecular Weight
43.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
