At5g41760 Antibody

Biological Context of At5g41760

The At5g41760 gene resides on chromosome 5 of Arabidopsis thaliana. While functional annotations for this gene remain partially uncharacterized, neighboring loci (e.g., AT5G41740 and AT5G41750) encode Toll/interleukin-1 receptor-nucleotide binding-leucine-rich repeat (TIR-NB-LRR) proteins critical for pathogen recognition and immune responses . These proteins often trigger hybrid necrosis when incompatible alleles interact, as demonstrated in studies of autoimmune-like responses in plant hybrids .

Antibody Development and Applications

Antibodies targeting plant proteins like At5g41760 are typically developed using:

• Immunogen Design: Recombinant proteins or synthetic peptides corresponding to unique epitopes of the At5g41760 protein.

• Host Systems: Polyclonal antibodies are commonly produced in goats or rabbits, while monoclonal versions use hybridoma or phage display technologies .

• Validation: Western blot (WB), immunofluorescence (IF), and ELISA are standard for specificity testing .

Research Findings and Challenges

• Immune Response Activation: Studies on adjacent TIR-NB-LRR genes (e.g., AT5G41740/AT5G41750) reveal that autoimmunity in hybrids involves temperature-sensitive activation of immune pathways . Antibodies against these proteins help map gene expression and protein localization during stress responses.

• Validation Criticality: Over 20% of commercial antibodies fail specificity tests, underscoring the need for knockout controls and orthogonal assays . For At5g41760, CRISPR-edited Arabidopsis lines would be essential to confirm antibody reliability.

• Structural Insights: Antibody-antigen binding depends on paratope-epitope complementarity, with framework regions (FRs) contributing up to 35% of binding energy in some cases .

Future Directions

• Proteome-Scale Projects: Initiatives like the EU Affinomics program highlight the demand for renewable, recombinant antibodies with open-access validation data .

• Therapeutic Potential: Engineered antibodies in plants could enable novel disease resistance strategies, akin to HIV-neutralizing antibodies like N6, which evade glycan steric hindrance .

Data Gaps and Recommendations