FUC95A Antibody

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Description

Introduction to FUC95A Antibody

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 .

Functional Role of FUC95A in XyG Remodeling

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:

EnzymeFunctionSubstrate SpecificityReferences
FUC95A (AXY8)Removes α-1,2-linked fucoseXyG fucosylation
MUR2Adds fucose to XyG via transferaseXyG fucosylation
BGAL10Removes galactose residuesXyG galactosylation

Auxin-Dependent XyG Remodeling

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 .

Epitope Mapping and Functional Studies

  • 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 .

Key Studies Using FUC95A Antibody

Study PurposeMethodsKey FindingsReferences
Auxin’s role in XyG remodelingGravistimulation, CCRC-M1 stainingAuxin asymmetry alters XyG fucosylation
FUC95A substrate specificityMutant analysis (e.g., mur2, axy8)FUC95A acts solely on XyG, not AGPs
Auxin regulation of XyG genesqPCR, YUC6 inductionFUC95A transcripts unchanged by auxin

Mechanistic Insights from FUC95A Research

FUC95A’s enzymatic activity is pivotal for balancing XyG cross-linking and loosening:

  • Fucose removal by FUC95A promotes XyG solubility, enabling cell wall relaxation during growth .

  • Auxin-independent regulation: Unlike MUR3 (galactosyltransferase), FUC95A transcription is not directly influenced by auxin, suggesting post-translational control .

Product Specs

Buffer
Preservative: 0.03% ProClin 300
Components: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
14-16 weeks (Made-to-order)
Synonyms
FUC95A antibody; AXY8 antibody; At4g34260 antibody; F10M10.30Alpha-L-fucosidase 2 antibody; EC 3.2.1.51 antibody; Alpha-1,2-fucosidase 2 antibody; Alpha-L-fucosidase 95A antibody; AtFuc95A antibody; Alpha-L-fucoside fucohydrolase 2 antibody; Protein ALTERED XYLOGLUCAN 8 antibody
Target Names
FUC95A
Uniprot No.

Target Background

Function
This antibody targets an enzyme that hydrolyzes alpha-1,2-linked fucose residues. It exhibits activity against fucosylated xyloglucan oligosaccharides but not against 3-fucosyllactose, p-nitrophenyl-alpha-L-fucopyranoside, lacto-N-fucopentaose II, lacto-N-fucopentaose III, or alpha-1,6-fucosylated chitopentaose. This enzyme is implicated in apoplastic xyloglucan metabolism.
Gene References Into Functions
  • Arabidopsis thaliana gene At4g34260 primarily acts on hemicellulose xyloglucan within the apoplast. PMID: 22080600
  • The Arabidopsis thaliana gene AtFuc95A plays a role in xyloglucan metabolism. PMID: 18495185
Database Links

KEGG: ath:AT4G34260

STRING: 3702.AT4G34260.1

UniGene: At.45833

Protein Families
Glycosyl hydrolase 95 family
Subcellular Location
Secreted, extracellular space, apoplast.
Tissue Specificity
Ubiquitous. Highest expression in vascular tissues, leaf trichomes, root elongation zone and emerging lateral roots.

Q&A

Here’s a structured collection of FAQs tailored for academic researchers investigating FUC95A (afucosylated IgG1) antibodies, synthesized from peer-reviewed studies and technical literature:

Advanced Research Questions

How should researchers resolve contradictions in FcγR-mediated activity across species?

  • Key conflict: Human afucosylated IgG1 binds mouse FcγRIV but not other murine FcγRs, limiting translatability of non-transgenic models .

  • Resolution strategy:

    • Use FcγR-humanized mice for in vivo studies .

    • Validate findings with primary human immune cells in ex vivo systems .

What methodologies optimize FUC95A for combination therapies?

  • Synergy with folate-drug conjugates: Co-administer FUC95A with FRβ-targeting agents (e.g., m909 antibody) to exploit non-overlapping epitopes and effector mechanisms .

    • Experimental workflow:

      • Pre-screen for FRβ/FcγR co-expression via dual-fluorescence staining .

      • Assess additive vs. synergistic effects using Bliss independence analysis .

How can FcγR polymorphisms impact FUC95A clinical trial design?

  • Critical factors:

    PolymorphismFunctional ImpactMitigation Strategy
    FCGR3A-158V/FAlters FcγRIIIa affinityStratify cohorts by genotype
    FCGR2A-131H/RReduces phagocytosisAdjust dosing or combine with Fc-engineered variants

Data Interpretation Guidelines

  • For ADCC variability: Normalize results to donor-specific NK cell activation thresholds (e.g., CD107a degranulation levels) .

  • For tumor model discrepancies: Cross-validate using orthotopic vs. metastatic models to isolate microenvironmental effects .

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