Recombinant Ceratophyllum demersum ATP synthase subunit c, chloroplastic (atpH)

Shipped with Ice Packs
In Stock

Description

Production and Purity

  • Recombinant proteins are lyophilized or stored in glycerol to prevent degradation.

  • Tags (e.g., His-tag) enhance purification via affinity chromatography .

Research Applications and Findings

Role in Mitochondrial Pathology
Recent studies highlight the c-subunit’s dual role:

Study FocusKey FindingsReferences
Mitochondrial Permeability Transition (mPT)- c-subunit ring forms a calcium-regulated pore.
- Overexpression sensitizes neurons to cell death.
Amyloidogenic Properties- Spontaneously folds into β-sheets and forms fibrils in Ca²⁺-dependent manner.
- Oligomers create ion-conductive pores in lipid bilayers.
Metabolic Dysregulation- Elevated free c-subunit levels correlate with reduced ATP synthesis efficiency.
- Linked to aberrant protein synthesis rates.

Mechanistic Insights

  • Gating Model: Conformational changes in ATP synthase subunits (e.g., e, g) modulate c-subunit pore opening .

  • Pathological Relevance: Misfolded c-subunit oligomers may contribute to lysosomal storage diseases or neurodegeneration .

Experimental Relevance

Recombinant Protein Uses

  • ELISA Assays: Detects atpH expression levels in plant tissues (e.g., Ceratophyllum demersum) .

  • Structural Studies: His-tagged versions enable crystallography or cryo-EM to resolve c-ring dynamics .

  • Functional Assays: Black lipid membrane experiments test pore-forming activity .

Challenges

  • Purification: Hydrophobicity necessitates specialized detergents (e.g., Genapol) .

  • 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
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-81
Protein Length
full length protein
Species
Ceratophyllum demersum (Rigid hornwort) (Coontail)
Target Names
atpH
Target Protein Sequence
MNPLISSASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFM EALTIYGLVVALALLFANPFV
Uniprot No.

Target Background

Function
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.
Protein Families
ATPase C chain family
Subcellular Location
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2025 TheBiotek. All Rights Reserved.