SPAC6G10.10c encodes a protein implicated in β-1,6-glucan synthesis and cell wall integrity in S. pombe. Polyclonal or monoclonal antibodies targeting this protein are custom-developed for research applications, enabling visualization, quantification, and functional disruption of the protein in yeast models. These antibodies are pivotal for understanding fungal pathogenesis and cell cycle regulation .
SPAC6G10.10c depletion disrupts β-1,6-glucan polymer formation, leading to cell wall fragility and compromised structural integrity.
Mutants exhibit malformed septa with aberrant accumulation of β-1,3-glucan, suggesting cross-talk between glucan synthase pathways .
Conditional knockdown of SPAC6G10.10c results in incomplete septum closure and abnormal cell morphology.
Transcriptomic analyses reveal upregulated expression of glucanases (e.g., Gas2p) and other cell wall repair enzymes in response to SPAC6G10.10c deficiency .
SPAC6G10.10c protein undergoes O-mannosylation, which masks an unconventional N-glycosylation site (N-X-A sequon).
In O-mannosylation-deficient strains (oma4Δ), N-glycosylation at this site becomes detectable, altering protein stability and function .
Antibodies against SPAC6G10.10c enable tracking of cell wall synthesis during infection models, aiding antifungal drug discovery.
Used to validate β-1,6-glucan as a therapeutic target in Candida and Aspergillus species .
Immunofluorescence with SPAC6G10.10c antibodies visualizes septum assembly defects in mutants, linking glucan metabolism to cytokinesis .
Facilitates studies on engineered yeast strains with modified glycosylation pathways for biopharmaceutical production .
Cross-Reactivity: Antibodies may recognize homologs in other fungi (e.g., S. cerevisiae Kre9), necessitating validation via knockout controls .
Storage: Stable at -80°C with carrier proteins (e.g., BSA) to prevent aggregation .