Aggregation: Tendency to form amyloid fibrils complicates monomer isolation.
Product Specs
Form
Lyophilized powder Please note: We will prioritize shipping the format that is currently in stock. However, if you have specific requirements for the format, please indicate them in your order notes, and we will fulfill your request to the best of our ability.
Lead Time
Delivery time may vary depending on the purchasing method and location. Please contact your local distributor for precise delivery timeframes. Please note: All of our proteins are shipped with standard blue ice packs by default. If you require dry ice shipping, please notify us in advance, as additional fees will apply.
Notes
Repeated freezing and thawing is not recommended. For optimal preservation, store working aliquots at 4°C for up to one week.
Reconstitution
We recommend briefly centrifuging the vial prior to opening to ensure the contents settle to the bottom. Please reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers may use this as a reference.
Shelf Life
The shelf life of the product is dependent on various factors, including storage conditions, buffer components, temperature, and the inherent stability of the protein itself.
Generally, the shelf life of the liquid form is 6 months at -20°C/-80°C. The shelf life of the lyophilized form is 12 months at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is recommended for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type will be determined during the manufacturing process.
The tag type is determined during production. If you have a specific tag type requirement, please inform us, and we will prioritize developing the specified tag.
Synonyms
atpH; ATP synthase subunit c, chloroplastic; ATP synthase F(0 sector subunit c; ATPase subunit III; F-type ATPase subunit c; F-ATPase subunit c; Lipid-binding protein
F(1)F(0) ATP synthase is responsible for synthesizing ATP from ADP in the presence of a proton or sodium gradient. This enzyme consists of two structural domains: F(1), which contains the extramembraneous catalytic core, and F(0), which contains the membrane proton channel. These domains are connected by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled to proton translocation through a rotary mechanism of the central stalk subunits. The c-ring, a homomeric complex of 10-14 subunits, constitutes the central stalk rotor element and interacts with the F(1) delta and epsilon subunits. This subunit plays a direct role in proton translocation across the membrane.