The YLL056C antibody is a specialized immunological reagent designed to target the YLL056C protein in Saccharomyces cerevisiae. This protein, encoded by the YLL056C gene, is implicated in pleiotropic drug resistance and zinc homeostasis . The antibody enables researchers to study the protein’s localization, expression levels, and functional interactions through techniques such as Western blotting, immunoprecipitation, and fluorescence microscopy .
The YLL056C protein is associated with:
Zinc ion transmembrane transport: Deletion of YLL056C in yeast confers resistance to both high and low zinc concentrations, suggesting a regulatory role in zinc homeostasis .
Detoxification: Exhibits NAD(P)H-dependent reductase activity, contributing to furfural and hydroxymethylfurfural (HMF) detoxification in lignocellulosic hydrolysates .
Transcriptional regulation: Co-expressed with genes involved in drug resistance, though its direct molecular mechanisms remain under investigation .
The antibody has been used to track YLL056C-GFP fusion proteins via confocal microscopy, confirming its localization to the endoplasmic reticulum (ER) and plasma membrane under varying zinc conditions .
Comparative studies using crude cell extracts revealed that YLL056C overexpression enhances specific reductase activity (9.5 U/mg for furfural reduction), outperforming related enzymes like Ykl071wp (3.38 U/mg) .
The antibody aids in characterizing strains with YLL056C deletions or overexpression, particularly in stress-response pathways linked to oxidative damage and cell wall integrity .
The YLL056C antibody has been validated using:
| Protein | Substrate | Specific Activity (U/mg) | Cofactor |
|---|---|---|---|
| YLL056C | Furfural | 9.5 | NADH |
| Ykl071wp | Furfural | 3.38 | NADPH |
| Yll056cwp | HMF | 0.47 | NADPH |
Data adapted from furfural detoxification studies .
YLL056C overexpression: Reduces intracellular reactive oxygen species (ROS) by 43% under furfural stress .
YLL056C deletion: Increases susceptibility to zinc toxicity but enhances resistance to pleiotropic drugs .
While the YLL056C antibody has proven reliable in S. cerevisiae studies, its cross-reactivity with orthologs in other fungi remains untested. Ongoing efforts focus on structural characterization of the protein’s zinc-binding domains and its interaction with transcription factors like Rim101 .
For rigorous experimental design, consult open antibody databases such as YCharOS and Addgene’s Antibody Data Hub, which provide standardized validation protocols .