Recombinant Mouse-ear cress 2-Cys peroxiredoxin BAS1, chloroplastic (BAS1)

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Code CSB-YP822134DOA
Abbreviation Recombinant Mouse-ear cress BAS1 protein
MSDS
Size $436
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
BAS1
Uniprot No.
Research Area
Others
Alternative Names
2-Cys peroxiredoxin A; 2-Cys peroxiredoxin BAS1; 2-Cys Prx A; BAS1; BAS1A_ARATH; chloroplastic; Thiol-specific antioxidant protein A
Species
Arabidopsis thaliana (Mouse-ear cress)
Source
Yeast
Expression Region
66-266aa
Target Protein Sequence
KAQADDLPLVGNKAPDFEAEAVFDQEFIKVKLSDYIGKKYVILFFYPLDFTFVCPTEITAFSDRHSEFEKLNTEVLGVSVDSVFSHLAWVQTDRKSGGLGDLNYPLISDVTKSISKSFGVLIHDQGIALRGLFIIDKEGVIQHSTINNLGIGRSVDETMRTLQALQYIQENPDEVCPAGWKPGEKSMKPDPKLSKEYFSAI
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
24.4 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
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.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

Recombinant Arabidopsis thaliana 2-Cys peroxiredoxin BAS1, chloroplastic (BAS1) is produced in a yeast expression system, covering the mature protein from amino acids 66 to 266. The protein is expressed with an N-terminal 6xHis-tag to aid in purification and detection. Purity exceeds 90% as verified by SDS-PAGE, which appears to ensure reliable results for research applications.

2-Cys peroxiredoxin BAS1 plays a critical role in redox regulation within chloroplasts of Arabidopsis thaliana. It's involved in detoxifying peroxides and maintaining cellular redox homeostasis. This protein serves as a valuable tool for studying oxidative stress responses and redox signaling pathways in plants. It may provide insights into plant physiology and stress tolerance mechanisms.

Potential Applications

Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.

Arabidopsis thaliana BAS1 is a chloroplastic 2-Cys peroxiredoxin that requires precise folding, disulfide bond formation, and proper oligomerization for its redox regulatory activity. The yeast expression system provides a eukaryotic environment that supports proper protein folding and disulfide bond formation, increasing the probability of correct folding compared to bacterial systems. However, as a chloroplast-targeted protein, BAS1 may require specific chloroplast-specific modifications or chaperones for optimal folding. The N-terminal 6xHis tag is relatively small but may potentially interfere with the protein's N-terminal structural organization. While yeast expression provides favorable conditions, experimental validation remains essential to confirm structural integrity and enzymatic activity.

1. Protein-Protein Interaction Studies Using His-Tag Pull-Down Assays

This application requires proper folding validation. Peroxiredoxin interactions within redox networks require precise tertiary structure. If correctly folded (verified), the protein is suitable for identifying physiological interaction partners in chloroplast redox systems. If misfolded/unverified, there is a high risk of non-specific binding or failure to identify genuine redox partner interactions.

2. Antibody Development and Validation

Antibody development relies primarily on antigenic sequence recognition. If correctly folded (verified), the protein excels for generating conformation-sensitive antibodies that recognize native BAS1 epitopes. If misfolded/unverified, it remains suitable for producing antibodies against linear epitopes, which are still valuable for detection applications in plant research.

3. Biochemical Characterization and Enzyme Kinetics Analysis

These studies are essential for determining folding status and functional competence. If correctly folded (verified), characterization provides reliable data on peroxidase activity, oligomerization state, and redox properties. If misfolded/unverified, analysis yields physical property data, but enzymatic assays will not reflect native activity.

4. Comparative Structural and Functional Studies

This application depends on correct folding validation. Meaningful comparative studies require native protein conformation. If correctly folded (verified), the protein enables valid comparisons with other plant peroxiredoxins. If misfolded/unverified, comparative analyses would yield misleading results about evolutionary relationships.

Final Recommendation & Action Plan

The yeast expression system provides favorable folding conditions for this plant peroxiredoxin, but experimental validation of structural integrity and enzymatic activity is essential before reliable use in functional studies. Begin with Application 3 (Biochemical Characterization) to assess folding quality through size-exclusion chromatography (oligomerization state), circular dichroism spectroscopy, and validate peroxidase activity using standard substrates like H₂O₂ or organic peroxides. If correct folding and enzymatic activity are verified, proceed cautiously with Applications 1 and 4 for interaction studies and comparative analyses. Application 2 (antibody development) can proceed immediately regardless of folding status. If misfolding is detected, limit applications to linear epitope antibody production and basic biophysical characterization, avoiding all functional interaction and comparative studies. For reliable BAS1 research, always include appropriate redox activity controls and consider using plant-based expression systems for complete chloroplast-specific modifications.

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Target Background

Function
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.
Gene References into Functions
  1. These quantitative data support a model where 2-CysPrx and Cyp20-3, by interaction, form a redox-sensitive regulatory module in the chloroplast which is under control of the photosynthesis-linked stromal pH value, the redox state and additional stromal protein factor(s).[2-CysPrx] PMID: 26872837
  2. Substitution of Cys for Ser at amino acid location 150 of the alpha-helix of 2-Cys Prx A regulates/enhances the dual peroxidase and chaperone enzymatic functions. [2-cysteine peroxiredoxin A] PMID: 26141131
  3. BAS1 and SOB7 act redundantly with respect to light promotion of cotyledon expansion, repression of hypocotyl elongation and flowering time in addition to other phenotypes not regulated by light. PMID: 15773851
Subcellular Location
Plastid, chloroplast.
Protein Families
Peroxiredoxin family, AhpC/Prx1 subfamily
Database Links

KEGG: ath:AT3G11630

STRING: 3702.AT3G11630.1

UniGene: At.22950

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