No indexed publications in PubMed, PMC, or EMBASE reference "FAO3" as a target antigen, antibody clone, or therapeutic candidate.
The term does not align with established nomenclature for antibodies (e.g., CD nomenclature, INN/WINN classifications) or glycoproteins.
Several closely named entities exist but are unrelated to "FAO3":
Anti-Fc antibodies (e.g., rheumatoid factors) target the crystallizable fragment (Fc) of IgG, implicated in autoimmune diseases like rheumatoid arthritis .
Anti-Fab antibodies recognize the antigen-binding fragment (Fab) and are linked to immune dysregulation in chronic infections .
FAO (Fatty Acid Oxidation): Source 6 identifies proteins associated with FAO (e.g., ApoE, ApoA4) in regulatory T cells, but no "FAO3" protein or antibody is cited.
The International Nonproprietary Names (INN) system and WHO guidelines standardize antibody naming (e.g., suffix "-mab" for monoclonal antibodies) . Examples from current research:
If "FAO3" refers to:
A Novel Epitope: No experimental data or structural studies validate its existence.
Typographical Error: Possible confusion with "Ana o 3" (cashew allergen) or "Fcα/μR" (Fc receptors).
Proprietary Research: Unpublished/undisclosed projects would lack peer-reviewed validation.
Here’s a structured collection of FAQs tailored for researchers working with FAO3 antibodies, synthesized from peer-reviewed methodologies and experimental data:
Methodological steps:
Perform knockout/knockdown controls in target cell lines to confirm absence of off-target binding .
Use blocking peptides (e.g., recombinant Ana o 3 antigen) to compete for antibody binding .
Validate via orthogonal techniques (e.g., ELISA vs. western blot) to rule out assay-specific artifacts .
| Parameter | ELISA | Immunofluorescence |
|---|---|---|
| Optimal Dilution | 1:1000 | 1:500–1:1000 |
| Cross-reactivity | Species-specific | Subcellular localization |
| Negative Control | BSA-blocked wells | Knockout cell lines |
Key considerations:
Fixation: Use 1% BSA/50% glycerol/PBS (pH 7.4) to stabilize antigen-antibody interactions .
Antigen density: Ensure 400 ng/mL recombinant Ana o 3 for standard curve accuracy .
Wash buffers: Include 0.05% Tween-20 to minimize nonspecific binding .
Analytical framework:
Compare structural contexts: Antibody-antigen interactions may vary between soluble (ELISA) and fixed (IF) states due to epitope accessibility .
Quantify avidity effects: Multivalent binding in immunofluorescence amplifies signal vs. monovalent ELISA .
Assess batch variability: Validate lot-to-lot consistency via SDS-PAGE (e.g., single heavy/light chain bands) .
Solutions for flow cytometry/cellular assays:
Use REAfin™ Antibodies with engineered Fc regions to eliminate Fcγ binding .
Pair with REA Control (S/I) antibodies to distinguish specific vs. nonspecific interactions .
Optimize antibody concentration to 1–5 µg/ml, as higher concentrations increase off-target risks .
Structural insights from nanobody studies:
Spacer length: PEG linkers ≥6,000 Da enable optimal IgE cross-linking on effector cells (e.g., 19% β-hexosaminidase release at 100 µM) .
Epitope geometry: Bivalent FAO3 formats (e.g., BiAns) improve immunocomplex stability vs. monovalent designs .
| Architecture | Spacer Length | Degranulation Efficiency |
|---|---|---|
| Monovalent FAO3 | N/A | <5% β-hexosaminidase |
| Bivalent BiAn(600) | 6 nm | 6.3% ring-closed complexes |
| Bivalent BiAn(6000) | 12 nm | 19% activity at 100 µM |
Guidelines from large-scale mining: