Analytical Data
-
Gene name
ATP6V0C
- Application
-
Alternative Names
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
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y487
-
Expression Region
1-155aa
-
AA Sequence
MSESKSGPEYASFFAVMGASAAMVFSALGAAYGTAKSGTGIAAMSVMRPEQIMKSIIPVVMAGIIAIYGLVVAVLIANSLNDDISLYKSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK
-
Molecular Weight
42.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
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.
