The FUC95A Antibody is a high-specificity monoclonal antibody targeting the FUC95A (AXY8) protein in Arabidopsis thaliana. This enzyme belongs to the glycosyl hydrolase family (GH95) and functions as a fucosylhydrolase, specifically removing α-1,2-linked fucose residues from xyloglucans (XyGs), a major component of plant cell walls . The antibody is widely used in plant biology to study XyG structural modifications, which influence cell wall elasticity, growth, and responses to environmental cues like auxin .
FUC95A (AXY8) is critical for modifying XyG structures by cleaving fucose side chains. This activity contrasts with other fucosyltransferases (e.g., MUR2) and galactosidases (e.g., BGAL10), which add or remove galactose residues, respectively . Key distinctions include:
Auxin regulates plant growth by altering XyG structures. A study using the CCRC-M1 antibody (detects fucosylated XyG epitopes) and FUC95A mutants revealed:
Auxin asymmetry (induced via gravistimulation) correlates with spatial changes in XyG fucosylation in dark-grown hypocotyls .
FUC95A mutants (e.g., axy8) showed no significant changes in auxin sensitivity compared to wild-type plants, indicating auxin does not directly regulate FUC95A transcription .
Target specificity: FUC95A exclusively acts on XyG fucosylation, not arabinogalactan proteins (AGPs) .
Enzyme activity: FUC95A’s removal of fucose enhances XyG solubility and cell wall extensibility, critical for growth responses .
FUC95A’s enzymatic activity is pivotal for balancing XyG cross-linking and loosening:
Here’s a structured collection of FAQs tailored for academic researchers investigating FUC95A (afucosylated IgG1) antibodies, synthesized from peer-reviewed studies and technical literature:
Key conflict: Human afucosylated IgG1 binds mouse FcγRIV but not other murine FcγRs, limiting translatability of non-transgenic models .
Resolution strategy:
Synergy with folate-drug conjugates: Co-administer FUC95A with FRβ-targeting agents (e.g., m909 antibody) to exploit non-overlapping epitopes and effector mechanisms .
Critical factors: