Recombinant Acorus calamus ATP synthase subunit c, chloroplastic (atpH)
Description
Molecular Structure and Properties
The ATP synthase subunit c (atpH) is a proteolipid that oligomerizes into a rotary c-ring structure embedded in thylakoid membranes. Key structural features include:
Recombinant Production and Purification
Recombinant production enables large-scale studies of this subunit’s biophysical and functional roles:
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Expression System: Typically produced in Escherichia coli with codon optimization for high yield .
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Tags: May include affinity tags (e.g., maltose-binding protein) during production .
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Storage: Stabilized in Tris-based buffer with 50% glycerol at –20°C .
Example Protocol (adapted from spinach homolog studies ):
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Clone synthetic atpH into pET vector.
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Express in E. coli BL21(DE3) with IPTG induction.
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Purify via affinity chromatography and ion-exchange steps.
Functional Role in Photosynthesis
The c-ring acts as a proton-driven rotor in ATP synthesis:
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Proton Translocation: Each c-subunit binds one proton, and the ring’s rotation drives ATP production in the F₁ sector .
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Stoichiometry Impact:
Table 1: Experimental Insights from Transplastomic Studies
Applications and Future Directions
Product Specs
Please note: We prioritize shipping the format currently in stock. However, if you require a specific format, please indicate your preference in the order notes. We will fulfill your request if available.
Note: All our proteins are shipped with standard blue ice packs. If you require dry ice shipping, please inform us in advance. Additional fees will apply.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
