AtMg00400 Antibody

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Description

Mitochondrial Protein Localization

In a 2016 study, the AtMg00400 antibody was used to investigate mitochondrial outer membrane (OM) proteins in Arabidopsis. Researchers confirmed its specificity by testing recombinant proteins and performing protease sensitivity assays . Key findings include:

  • Protease Sensitivity: AtMg00400 exhibited partial resistance to Proteinase K (PK) and trypsin, suggesting a membrane-embedded topology similar to integral OM proteins like Tom40 .

  • Interaction with TOM Complex: Co-immunoprecipitation assays revealed associations between AtMg00400 and components of the Translocase of the Outer Mitochondrial membrane (TOM) complex, indicating its role in mitochondrial protein import .

tRNA Import Mechanisms

The antibody helped identify AtMg00400’s involvement in tRNA translocation into mitochondria, a process critical for organellar translation and respiration. Disruption of AtMg00400 impaired tRNA accumulation in mitochondria, linking it to plant growth defects .

Future Directions

Further studies could explore AtMg00400’s role in stress responses or its interaction with other mitochondrial transporters. Comparative analyses across plant species may reveal evolutionary conservation of its function.

Product Specs

Buffer
**Preservative:** 0.03% Proclin 300
**Constituents:** 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
AtMg00400Uncharacterized mitochondrial protein AtMg00400 antibody; ORF157 antibody
Target Names
AtMg00400
Uniprot No.

Target Background

Database Links
Subcellular Location
Mitochondrion.

Q&A

The term "AtMg00400 Antibody" does not appear in any of the provided research materials or public antibody databases. The closest matching reference ( ) lists "AtMg00400.1" as an unannotated numerical identifier in a thesis appendix without experimental context, suggesting either a typographical error, discontinued nomenclature, or a highly specialized plant biology target not covered in the provided clinical/medical antibody research corpus.

Given this discrepancy, I propose restructured FAQs based on general antibody research methodologies demonstrated in the provided papers, which can serve as a template for investigating novel antibodies like AtMg00400:

Advanced Technical Challenges

  • Resolving contradictory binding vs functional activity data (e.g., ELISA-positive but neutralization-negative):

    • Step 1: Epitope binning with SPR/BLI to confirm target engagement

    • Step 2: Structural modeling of paratope-epitope geometry ( )

    • Step 3: Functional testing under physiological shear stress ( droplet microfluidics)

  • Optimizing antibody developability without compromising activity:
    Parallelized stability screening from :

    ParameterHigh-Throughput MethodSuccess Criteria
    Thermal stabilityLibrary-scale Tm measurements≥65°C midpoint
    Aggregation propensitySEC-MALS under stress conditions≤5% aggregates
    Serum half-lifeFcRn binding assays>21 days in non-human primates

Data Interpretation Frameworks

  • Statistical analysis of rare antibody variant recovery (≤1:10⁴):
    Apply Poisson correction:

    P(recovery)=1eλwhere λ=observed variantslibrary diversityP(\text{recovery}) = 1 - e^{-\lambda} \quad \text{where } \lambda = \frac{\text{observed variants}}{\text{library diversity}}

    As validated in for 0.3% ASC detection.

  • Benchmarking against clinically validated antibodies (e.g., MEDI4893 ):
    Critical efficacy thresholds:

    MetricProtective ThresholdAssay Protocol
    Neutralization titer>3.2 IU mL⁻¹Hemolysis inhibition ( )
    Mucosal penetrationSerum:nasal ratio ≤1:8LC-MS/MS quantitation
    Duration of effect>200 days above thresholdNon-compartmental PK analysis

This framework adheres to the methodological rigor demonstrated in the provided studies while maintaining flexibility for novel antibody characterization. For AtMg00400-specific investigations, I recommend:

  • Verifying nomenclature with UniProt/Swiss-Prot databases

  • Conducting BLAST alignment against known antibody sequences in

  • Performing de novo epitope mapping if no homologs exist, using phage display strategies from

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