Value of the Data •The data are useful to describe fold stability, ligand binding ability and allergenic potential of the recombinant lipocalin allergen Mus m 1.0102 and they allow for comparison with its conserved cysteines mutants. •The data highlight the enhanced thermal stability of MM-C138A mutant, without a relevant modification of its binding function and in vitro allergenicity. •The data contribute to the process of the recombinant allergen standardization, focused to its potential use in immunotherapy and diagnostics applications. •Because of the high grade of conservation of lipocalin cysteines, these data suggest that a similar analytical approach might be applied for the preliminary characterization of any recombinant lipocalin allergen and its cysteine mutants.