Analytical Data
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Gene name
ATP6AP1
- Application
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Alternative Names
ATP6AP1; ATP6IP1; ATP6S1; VATPS1; XAP3; V-type proton ATPase subunit S1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15904
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Expression Region
1-470aa
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AA Sequence
MMAAMATARVRMGPRCAQALWRMPWLPVFLSLAAAAAAAAAEQQVPLVLWSSDRDLWAPAADTHEGHITSDLQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAVSTLTTYLQEKLGASPLHVDLATLRELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVARDVAVVAGGLGRQLLQKQPVSPVIHPPVSYNDTAPRILFWAQNFSVAYKDQWEDLTPLTFGVQELNLTGSFWNDSFARLSLTYERLFGTTVTFKFILANRLYPVSARHWFTMERLEVHSNGSVAYFNASQVTGPSIYSFHCEYVSSLSKKGSLLVARTQPSPWQMMLQDFQIQAFNVMGEQFSYASDCASFFSPGIWMGLLTSLFMLFIFTYGLHMILSLKTMDRFDDHKGPTISLTQIV
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Molecular Weight
78.4 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
ATP6AP1, or ATPase H+ transporting accessory protein 1, plays a critical role in the functioning of vacuolar H+-ATPases (V-ATPases), which are essential for maintaining cellular pH, ion homeostasis, and various endocytic processes. The protein is encoded by the ATP6AP1 gene located on chromosome X and is known to interact with the Vo domain of V-ATPases, facilitating their assembly and activity. Mutations in the ATP6AP1 gene have been linked to various diseases, including renal tubular acidosis, neurodevelopmental disorders, and specific immunological defects, highlighting its significant role in human health. Researchers have increasingly focused on the recombinant expression of ATP6AP1 to study its structure-function relationship, interaction with other V-ATPase subunits, and its involvement in disease mechanisms. By producing this protein in heterologous systems, scientists aim to better understand its biochemical properties and explore its potential as a therapeutic target. The characterization of ATP6AP1 also offers insights into the regulatory mechanisms of V-ATPase complexes, which are crucial for developing new strategies for treating related diseases. As a result, the study of ATP6AP1 and its recombinant forms is gaining momentum in the fields of biochemistry and molecular biology, creating opportunities for advancements in both basic research and clinical applications.
