Analytical Data
-
Gene name
ATP6V1E1
- Application
-
Alternative Names
ATP6V1E1; ATP6E; ATP6E2; V-type proton ATPase subunit E 1; V-ATPase subunit E 1
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P36543
-
Expression Region
1-226aa
-
AA Sequence
MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMNQARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCRKQDFPLVKAAVQKAIPMYKIATKNDVDVQIDQESYLPEDIAGGVEIYNGDRKIKVSNTLESRLDLIAQQMMPEVRGALFGANANRKFLD
-
Molecular Weight
50.6 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
ATP6V1E1, a subunit of the vacuolar ATPase (V-ATPase) complex, plays a crucial role in various cellular processes, including acidification of organelles, ion transport, and cellular pH regulation. Research has increasingly focused on ATP6V1E1 due to its involvement in several physiological and pathological conditions, such as cancer, neurodegenerative diseases, and metabolic disorders. Its expression levels and function may influence the progression of tumors and the viability of cancer cells, making it a potential biomarker and therapeutic target. Furthermore, dysfunction of V-ATPases, in which ATP6V1E1 is integral, has been linked to impaired cellular processes and pathologies. Thus, studying the recombinant protein ATP6V1E1 provides valuable insights into its structural and functional characteristics, enabling researchers to understand its role in health and disease more comprehensively. Advances in recombinant protein technology allow for the production of ATP6V1E1 in various systems, facilitating in-depth analyses, including enzymatic activity assays, structural studies, and drug interaction screenings. Overall, this research not only enhances our understanding of ATP6V1E1's biological significance but also opens avenues for developing novel therapeutic strategies targeting V-ATPase-related pathways.
