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Koppelman et al (2018) Release of Major Peanut Allergens from Their Matrix under Various pH and Simulated Saliva Conditions—Ara h2 and Ara h6 Are Readily Bio-Accessible. Nutrients 10(9) 1281 PMID: 30208580
Li et al (2010) Primary sequence and site-selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2. Protein Sci. 19(1) 174 PMID: 19937656
Percival et al (2016) Reproducibility of serum IgE, Ara h2 skin prick testing and fraction of exhaled nitric oxide for predicting clinical peanut allergy in children. Allergy Asthma Clin. Immunol. 12(1) PMID: 27499764
Ara h 2 is one of the major allergenic proteins from peanut (Arachis hypogaea) which contains approximately 13 potential allergenic proteins.
Ara h 2 is a member of the 2S albumins (conglutinins) belonging to the prolamin superfamily which also includes Ara h 6. 2S albumins contain major food allergens from seeds of many mono‐ and dicotyledon plants and share a common compact structure that renders the proteins highly resistant to proteolysis.
In mouse models Ara h 2 and Ara h 6 are the main cause of effector responses such as mast cell degranulation and anaphylaxis. Ara h 2 has a high predictive value for diagnosis of clinical peanut allergy and is also more potent than Ara h 1 or Ara h 3 in histamine release assays and skin prick tests.
This peptide represents a tryptic peptide of Ara h 2.
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