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Literature summary for 3.4.22.65 extracted from

  • Takai, T.; Kato, T.; Yasueda, H.; Okumura, K.; Ogawa, H.
    Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: Major conformational IgE epitopes blocked by prodomains (2005), J. Allergy Clin. Immunol., 115, 555-563.
    View publication on PubMed
Search for more literature for 3.4.22.65

Application

Application Comment Organism
medicine allergen is associated with allergic diseases such as bronchial asthma, rhinitis, and atopic dermatitis Dermatophagoides pteronyssinus
medicine prodomains of Der f 1 reduce allergenicity, decreased activity of the proforms in inhibiting IgE binding, proforms exhibit different secondary structures than the mature forms, major conformational IgE epitopes commonly found in a broad population of patients exist within the 2 regions blocked by the prosegments, results basis for allergen standardization and design of safer and more effective allergen vaccines Dermatophagoides farinae

Cloned(Commentary)

Cloned (Comment) Organism
recombinant proforms secreted into culture supernatant of Pichia pastoris cells and converted into prosequence-removed mature form Der p 1-WT Dermatophagoides pteronyssinus
recombinant proforms were secreted into the culture of Pichia pastoris transfectant cells and converted into the prosequence-removed mature forms by means of dialysis against an acidic buffer Dermatophagoides farinae

Protein Variants

Protein Variants Comment Organism
additional information mutant Der f 1-N53Q, in which the N-glycosylation motif within the mature sequence is disrupted Dermatophagoides farinae
N52Q mutant with disrupted N-glycosylation motif in the prodomain, lower productivity Dermatophagoides pteronyssinus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
17000
-
 Der f 1-N53Q, gel filtration Dermatophagoides farinae
17000 18000 recombinant form without N-glycosylation, gel filtration Dermatophagoides pteronyssinus
18000
-
 natural Der f 1, gel filtration Dermatophagoides farinae
25000
-
 nature form, gel filtration Dermatophagoides pteronyssinus

Organism

Organism UniProt Comment Textmining
Dermatophagoides farinae
-
-
-
Dermatophagoides pteronyssinus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
anion exchange and gel filtration Dermatophagoides pteronyssinus
mature forms were purified by anion-exchange and gel filtration chromatography, proforms were purified by means of the same methods as the mature forms but without activation by dialysis against acidic buffer, natural Der f 1 was purified from whole culture extracts of Dermatophagoides farinae Dermatophagoides farinae

Subunits

Subunits Comment Organism
monomer SDS-PAGE Dermatophagoides farinae
monomer 1 * 17000-18000, gel filtration and SDS-PAGE Dermatophagoides pteronyssinus

Synonyms

Synonyms Comment Organism
Der f 1
-
 Dermatophagoides farinae
Der p 1
-
 Dermatophagoides pteronyssinus
major house dust mite allergen
-
 Dermatophagoides pteronyssinus