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Recombinant pro‐Der p 1 expressed in yeast Pichia pastoris was convertible into the prosequence‐removed mature Der p 1 with full activities of cysteine protease and IgE‐binding with or without N‐glycosylation of the mature sequence as well as pro‐Der f 1. The active recombinant variants will be the basis for various future studies. The major N‐terminus of pro‐Der p 1 with low proteolytic activity was the putative signal‐cleavage site, while that of pro‐Der f 1 contained not only the equivalent site but also 21 residues downstream, and pro‐Der f 1 retained significant activity. Contribution of the N‐terminal region of the Der p 1 prosequence including an N‐glycosylation motif on effective inhibition of proteolytic activity of pro‐Der p 1 was suggested.