Recombinant Struthio camelus ATP synthase subunit a (MT-ATP6)

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Description

Key Functions:

  • Proton Translocation: Forms part of the c-ring, enabling efficient proton movement .

  • Dimerization and Stabilization: Interacts with subunits b, e, and A6L to stabilize the F₀–F₁ interface and promote dimerization of ATP synthase complexes .

  • Rotary Mechanism: Directly participates in the rotational motion required for ATP production .

Research Applications and Biochemical Findings

MT-ATP6 is used in studies of mitochondrial disorders and ATP synthase dysfunction. Key findings include:

Table 1: Biochemical Anomalies in MT-ATP6 Variants

MutationBiochemical AnomalyProposed Mechanism
m.8993T>GReduced ATP synthesis, increased membrane potentialImpaired proton discharge, uncoupling of ATP synthesis
m.9185T>CDecreased membrane potential, impaired assemblyUnregulated proton leak, destabilized F₀–F₁ interface
m.8618insTDecreased ATPase activity, unstable holoenzymeSubunit a degradation, disrupted F₀ structure

Disease Associations:

  • NARP Syndrome: Caused by mutations in MT-ATP6, leading to ATP synthesis deficits .

  • Mitochondrial Spastic Paraplegia: Linked to impaired subunit a production .

Challenges and Future Directions

  • Assembly Complexity: Full-length MT-ATP6 requires precise folding and interaction with nuclear-encoded subunits (e.g., A6L, ATP8) .

  • Therapeutic Potential: Recombinant MT-ATP6 may aid in studying gene therapy for mitochondrial diseases .

Product Specs

Form
Lyophilized powder
Note: While we strive to ship the format currently in stock, we understand your specific needs. If you require a particular format, please indicate your preference during the order process, and we will accommodate your request.
Lead Time
Delivery times may vary depending on the purchasing method and location. Please consult your local distributor for specific delivery timelines.
Note: Our proteins are shipped with standard blue ice packs by default. If you require dry ice shipping, please inform us in advance. An additional fee will apply.
Notes
Repeated freezing and thawing is not recommended. For optimal stability, store working aliquots at 4°C for up to one week.
Reconstitution
We recommend centrifuging the vial briefly before opening to ensure the contents settle at the bottom. Reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting the solution at -20°C/-80°C. Our standard glycerol concentration is 50%, which you can use as a reference.
Shelf Life
The shelf life of our products is influenced by various factors including storage conditions, buffer composition, temperature, and the protein's inherent stability.
Generally, the shelf life of liquid protein is 6 months at -20°C/-80°C. For lyophilized protein, the shelf life is 12 months at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquot the protein for multiple uses. Avoid repeated freeze-thaw cycles to maintain product integrity.
Tag Info
Tag type will be determined during the manufacturing process.
The tag type is determined during production. If you have a specific tag requirement, please inform us, and we will prioritize its development.
Synonyms
MT-ATP6; ATP6; ATPASE6; MTATP6; ATP synthase subunit a; F-ATPase protein 6
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-227
Protein Length
full length protein
Species
Struthio camelus (Common ostrich)
Target Names
Target Protein Sequence
MNLSFFDQFASPQLLGIPLILLSLLFPTLLLPSPNNRWINNRLSTLQLWFLQLITKQLMM PLNKAGHKWALILTSLMTFLLLINLLGLLPYTFTPTTQLSMNMALAFPLWLATLLTGLRN QPSISLGHLLPEGTPTPLIPALILIETTSLLIRPLALGVRLTANLTAGHLLIQLISTATL ALLPTMPTISVLTATVLLLLTILELAVAMIQAYVFVLLLSLYLQENI
Uniprot No.

Target Background

Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) generates ATP from ADP in the presence of a proton gradient across the membrane, which is produced by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains: F(1), containing the extramembraneous catalytic core, and F(0), containing the membrane proton channel. These domains are linked by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the F(1) catalytic domain is coupled to proton translocation via a rotary mechanism involving the central stalk subunits. As a key component of the proton channel, this subunit may play a direct role in the translocation of protons across the membrane.
Protein Families
ATPase A chain family
Subcellular Location
Mitochondrion inner membrane; Multi-pass membrane protein.

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