DALL2 Antibody

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Description

Functional Insights from TAA Studies

TAAs like SadA (Salmonella), EhaG (EHEC), and UpaG (UPEC) rely on DALL2 domains to:

  • Project adhesive heads away from the bacterial surface.

  • Mediate transitions between coiled-coil stalks and β-structured anchors.

  • Enhance mechanical stability against host immune defenses .

Antibodies targeting DALL2 disrupt these functions, as evidenced by:

  • Reduced bacterial adhesion in Salmonella mutants lacking intact DALL2 domains.

  • Impaired immune evasion in UPEC strains with DALL2 mutations .

Research Tools

  • Structural Mapping: Anti-DALL2 antibodies localize TAAs in electron microscopy (e.g., anti-SadA antibodies in Salmonella) .

  • Functional Blockade: Neutralizing DALL2 antibodies inhibit TAA-mediated host cell binding in E. coli and Salmonella .

Therapeutic Potential

While no clinical trials target DALL2 directly, advances in AI-driven antibody design (e.g., AF2Complex, ImmuneBuilder) suggest pathways for engineering high-affinity DALL2 blockers . For example:

  • AI-Optimized Affinity: Stanford researchers improved antibody efficacy 25-fold against viral targets using structural data .

  • Cross-Reactivity Mitigation: Computational tools like MAbSilico predict off-target binding risks for DALL2 antibodies .

Challenges and Future Directions

  • Epitope Accessibility: The DALL2 domain’s buried location in TAAs complicates antibody binding .

  • Antigenic Variability: TAAs exhibit high genetic diversity across bacterial strains, necessitating broad-spectrum antibody designs .

  • AI Integration: Combining deep learning (e.g., AlphaFold2) with high-throughput screening could accelerate DALL2 antibody discovery .

Key Research Findings

StudyMethodOutcomeReference
SadA structure determinationX-ray crystallographyDALL2 stabilizes β-sheet continuity in neck domains
TAA functional analysisElectron microscopyDALL2 deletion reduces bacterial adhesion
AI-driven antibody designDeep learning (AF2Complex)Predicted antibody-antigen interactions with 90% accuracy

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Composition: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
14-16 week lead time (made-to-order)
Synonyms
At1g51440 antibody; F5D21.19 antibody; Phospholipase A1-Igamma3 antibody; chloroplastic antibody; EC 3.1.1.- antibody
Target Names
DALL2
Uniprot No.

Target Background

Function

This antibody targets an acylhydrolase enzyme. The enzyme catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. It exhibits moderate activity towards phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), and triacylglycerol (TAG).

Database Links

KEGG: ath:AT1G51440

STRING: 3702.AT1G51440.1

UniGene: At.18291

Protein Families
AB hydrolase superfamily, Lipase family
Subcellular Location
Plastid, chloroplast.
Tissue Specificity
Highly expressed in flowers. Lower levels in seedlings, leaves and stems.

Q&A

Here’s a structured collection of FAQs for researchers working with DALL2 antibodies, optimized for academic research scenarios and based on scientific literature:

How is DALL2 identified and validated in structural studies?

DALL2 is identified through cryo-EM or X-ray crystallography to resolve its β-sheet architecture and interactions. Validation involves:

  • Structural alignment: Comparing resolved DALL2 domains (e.g., β-strand arrangements) with reference structures from databases like PDB .

  • Mutagenesis: Disrupting conserved residues (e.g., tryptophan or histidine) to assess impact on β-sheet stability .

  • Cross-reactivity assays: Testing against related domains (e.g., DALL1) to confirm specificity .

What protocols ensure reliable DALL2 antibody performance?

  • Storage: Lyophilized antibodies should be stored at -20°C with stabilizers (e.g., recombinant BSA) to prevent aggregation .

  • Working concentrations:

    ApplicationPurified Antibody Concentration
    Western Blot1–5 µg/ml
    Immunoprecipitation5–10 µg/ml
    Structural Studies10–20 µg/ml (for cryo-EM grids)

How do I distinguish DALL2 from homologous domains like DALL1?

  • Epitope mapping: Use peptide arrays or hydrogen-deuterium exchange mass spectrometry to identify binding regions unique to DALL2 .

  • Structural comparison: Analyze β-sheet spacing (DALL2 lacks the water-mediated insertion seen in DALL1) .

How to resolve contradictions between predicted and observed DALL2 epitopes?

  • Integrate AI predictions with experimental validation:

    • Use tools like AF2Complex (deep learning) to predict antibody-antigen interfaces .

    • Validate with cryo-EM to confirm spatial binding (e.g., AI-predicted vs. actual β-sheet interactions) .

  • Statistical analysis: Compare computational confidence scores (e.g., pLDDT >90) with experimental resolution (<3.0 Å) .

What methods optimize DALL2 antibody affinity without germline bias?

  • Language model-guided mutagenesis:

    • Train models (e.g., AbLang-2) on nongermline mutations to suggest substitutions in CDRs .

    • Prioritize residues with high positional entropy (e.g., solvent-exposed tryptophan in β-sheets) .

  • Affinity maturation: Combine error-prone PCR and yeast display to screen for Kd <10 nM variants .

How to design experiments evaluating DALL2’s role in pathogenicity?

  • Functional assays:

    • Co-immunoprecipitation: Identify DALL2 interaction partners (e.g., host extracellular matrix proteins) .

    • Neutralization assays: Test antibody efficacy in blocking DALL2-mediated adhesion (e.g., in Salmonella models) .

  • Data interpretation: Use structural insights (e.g., β-sheet flexibility) to explain variable neutralization outcomes .

Methodological Considerations

  • Cross-reactivity mitigation: Pre-adsorb antibodies against DALL1 peptides to reduce off-target binding .

  • Data validation: Always pair computational predictions (e.g., AF2Complex) with orthogonal techniques like SPR or BLI .

  • Ethical reporting: Disclose unresolved contradictions (e.g., AI vs. structural data) in publications to guide future studies .

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