The At4g17565 gene encodes a putative F-box protein, a component of E3 ubiquitin ligase complexes that regulate protein ubiquitination and subsequent degradation. The antibody is specifically raised against a recombinant At4g17565 protein and is used to study its expression and function in Arabidopsis thaliana .
F-box proteins are modular scaffolds that recruit substrate proteins to the SCF (SKP1-CUL1-F-box) complex, directing their ubiquitination. While the precise function of At4g17565 remains under investigation, F-box proteins in plants are often implicated in:
Protein turnover during stress responses (e.g., temperature, drought).
Developmental regulation (e.g., flowering time, cell differentiation).
The antibody is primarily employed in Western Blot (WB) and ELISA assays to detect and quantify At4g17565 protein levels in Arabidopsis tissues. Potential research applications include:
Studying protein degradation pathways in abiotic stress responses.
Investigating developmental regulation (e.g., flowering time, senescence).
Analyzing gene expression in transgenic or mutant Arabidopsis lines .
The antibody is highly specific to At4g17565 in Arabidopsis thaliana, with no reported cross-reactivity to homologs in other species. This specificity is critical for minimizing false positives in downstream analyses .
While F-box protein antibodies vary in target specificity and reactivity, the At4g17565 Antibody distinguishes itself through:
Arabidopsis-specific reactivity, unlike antibodies targeting conserved F-box domains in animals or pathogens .
Focus on plant biology, contrasting with antibodies for human F-box proteins (e.g., MAX.16H5 for CD4 ).
Polyclonal design, offering broader epitope recognition compared to monoclonal alternatives .
Despite its utility, gaps remain in understanding At4g17565’s functional role. Future studies could:
Map epitopes to identify conserved regions for cross-species applications.
Explore interactions with SCF complex components (e.g., SKP1, CUL1).
Investigate stress-induced regulation via quantitative proteomics.