Recombinant Alocasia macrorrhizos Ferredoxin-B

Shipped with Ice Packs
In Stock

Product Specs

Form
Lyophilized powder. Note: We will prioritize shipping the format currently in stock. If you have specific format requirements, please note them when ordering, and we will fulfill your request.
Lead Time
Delivery times vary based on purchasing method and location. Please consult your local distributor for specific delivery information. Note: All proteins are shipped with standard blue ice packs. For dry ice shipping, please contact us in advance; additional charges will apply.
Notes
Avoid repeated freezing and thawing. Working aliquots can be stored at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening to collect contents at the bottom. Reconstitute the protein in sterile deionized 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 standard final glycerol concentration is 50% for your reference.
Shelf Life
Shelf life depends on several factors including storage conditions, buffer components, storage temperature, and protein stability. Generally, the liquid form has a shelf life of 6 months at -20°C/-80°C, while the lyophilized form has a shelf life of 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon arrival. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type will be determined during the manufacturing process. If you require a specific tag type, please inform us, and we will prioritize developing it.
Synonyms
Ferredoxin-B; Fd B
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-98
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Alocasia macrorrhizos (Giant taro) (Arum macrorrhizon)
Target Protein Sequence
ATYKVKLVTP SGQPLEFECP DDVYILDQAE EEGIDLPYSC RAGSCSSCAG KVKNGNVDQS DGSFLDDDQI GEGWVLTCVA YPTSDVVIET HKEEELTA
Uniprot No.

Target Background

Function
Ferredoxins are iron-sulfur proteins involved in electron transfer in various metabolic reactions.
Protein Families
2Fe2S plant-type ferredoxin family
Subcellular Location
Plastid, chloroplast.

Q&A

Experimental Design for Studying Recombinant Ferredoxins

When designing experiments to study recombinant ferredoxins, several factors must be considered, including expression systems, purification methods, and functional assays.

Question: What are the key considerations for designing an experiment to express and characterize recombinant Alocasia macrorrhizos ferredoxin-B?

Answer:

  • Expression System: Choose an appropriate host organism (e.g., E. coli, yeast) based on the protein's complexity and the desired yield.

  • Purification Method: Select methods like affinity chromatography or gel filtration to ensure high purity.

  • Functional Assays: Use spectroscopic methods (e.g., UV-Vis) to assess the protein's redox properties and electron transfer capabilities.

Data Analysis and Contradiction Resolution

In research, data analysis often involves resolving contradictions between expected and observed results.

Question: How can researchers resolve contradictions between theoretical models of ferredoxin function and experimental data showing unexpected redox properties in recombinant Alocasia macrorrhizos ferredoxin-B?

Answer:

  • Re-evaluate Assumptions: Check if the theoretical models accurately reflect the specific conditions under which the experiments were conducted.

  • Experimental Validation: Perform additional experiments to validate the observed properties, such as using different buffers or temperatures.

  • Literature Review: Compare findings with similar studies on other ferredoxins to identify potential explanations for the discrepancies.

Advanced Research Questions: Structural and Functional Insights

Advanced research often focuses on detailed structural and functional analyses of proteins.

Question: What structural features of recombinant Alocasia macrorrhizos ferredoxin-B might influence its electron transfer efficiency, and how can these be studied?

Answer:

  • Structural Analysis: Use techniques like X-ray crystallography or NMR spectroscopy to determine the protein's structure.

  • Mutagenesis Studies: Perform site-directed mutagenesis to alter specific residues and assess their impact on electron transfer efficiency.

  • Biochemical Assays: Conduct kinetic studies to measure the rates of electron transfer reactions.

Methodological Considerations for Biochemical Characterization

Biochemical characterization involves assessing the protein's stability, activity, and interactions with other molecules.

Question: What methodological approaches can be used to characterize the biochemical properties of recombinant Alocasia macrorrhizos ferredoxin-B?

Answer:

  • Stability Assays: Use thermal shift assays or circular dichroism to assess thermal stability.

  • Activity Assays: Employ spectroscopic methods to monitor electron transfer reactions.

  • Interaction Studies: Utilize techniques like co-immunoprecipitation or surface plasmon resonance to study interactions with other proteins.

Implications for Plant Biotechnology

Understanding ferredoxins can have implications for improving plant metabolism and stress tolerance.

Question: How might insights from studying recombinant Alocasia macrorrhizos ferredoxin-B contribute to plant biotechnology, particularly in enhancing stress tolerance or photosynthetic efficiency?

Answer:

  • Gene Editing: Use CRISPR/Cas9 to introduce modifications that enhance ferredoxin function in plants, potentially improving stress tolerance or photosynthetic efficiency.

  • Biotechnological Applications: Explore the use of ferredoxin in bioelectrochemical systems or as a component in biofuel cells.

Ethical and Regulatory Considerations

When applying biotechnological advancements, ethical and regulatory considerations are crucial.

Question: What ethical and regulatory frameworks should researchers consider when developing biotechnological applications involving recombinant Alocasia macrorrhizos ferredoxin-B?

Answer:

  • Regulatory Compliance: Ensure compliance with local and international regulations regarding genetically modified organisms (GMOs).

  • Ethical Review: Conduct ethical reviews to assess potential environmental impacts and societal implications of the technology.

Future Directions in Ferredoxin Research

Future research directions may involve integrating ferredoxins into novel biotechnological systems.

Question: What future research directions might be most promising for recombinant Alocasia macrorrhizos ferredoxin-B, particularly in emerging biotechnologies?

Answer:

  • Bioelectrochemistry: Explore the integration of ferredoxin into bioelectrochemical systems for energy applications.

  • Synthetic Biology: Design novel metabolic pathways incorporating ferredoxin to enhance photosynthetic efficiency or produce valuable chemicals.

Collaborative Research Opportunities

Collaboration across disciplines can enhance research outcomes.

Question: How can researchers from different fields collaborate effectively to advance our understanding and application of recombinant Alocasia macrorrhizos ferredoxin-B?

Answer:

  • Interdisciplinary Workshops: Organize workshops to bring together experts in biochemistry, biotechnology, and plant biology.

  • Joint Research Projects: Develop collaborative projects that integrate expertise from multiple disciplines to tackle complex research questions.

Educational Resources and Training

Providing educational resources is essential for advancing research capabilities.

Question: What educational resources or training programs would be beneficial for researchers interested in studying recombinant ferredoxins like Alocasia macrorrhizos ferredoxin-B?

Answer:

  • Workshops and Courses: Offer hands-on training in protein expression, purification, and characterization techniques.

  • Online Resources: Develop webinars or tutorials on advanced biochemical and biophysical methods for protein analysis.

Data Tables and Research Findings

While specific data tables for "Recombinant Alocasia macrorrhizos Ferredoxin-B" are not available due to the lack of direct literature, researchers can draw from studies on similar ferredoxins to inform their experimental design and data analysis. For example, studies on the overexpression of ferredoxin-NADP+ reductase in non-photosynthetic tissues can provide insights into the biochemical properties of ferredoxins in general .

Ferredoxin PropertyMethod of AnalysisExpected Outcome
Redox PotentialCyclic VoltammetryDetermine electron transfer capabilities
StabilityThermal Shift AssaysAssess thermal stability
Electron Transfer RateKinetic SpectroscopyMeasure rates of electron transfer reactions

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