Fc engineering
Identify Fc residues and compare candidate constructs.
Results
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Method & evidence
Map source sequences to human IgG references and apply explicit Fc designs while preserving the supplied Fab.
Scope & limitations
- Human IgG reference context; variable-domain numbering remains a separate analysis.
- Sequence alone cannot establish glycans, aggregation, receptor binding, or clinical half-life.
- Reference-structure contacts describe deposited complexes, not predicted variant effects.
Interpreting results
- Residue-set compatibility does not establish engineering history or biological activity.
- Reference differences may reflect allotype, engineering, or unresolved identity.
- Inspect each chain of an asymmetric antibody separately.
References
Input requirements & outputs
Input checks
- 30–1,500 unambiguous amino acids per chain
- Up to 100 rows and 60,000 residues in one native cohort
- Candidate construction requires complete, unambiguous, compatible Fc mapping
Expected results
- Observed EU residue map — Coverage, reference differences, missing positions, and uncertainty for each chain.
- Candidate sequences — Applied Fc edits, unchanged non-Fc residues, and exact input/output sequence identities.
- Per-row outcomes — Successful mappings and explicit failures retained together with source attribution.
