Allergen: | rAra h 2.0201 (Arachis hypogaea allergen 2) Glycosylation site N127 mutated (N127Q |
Unit: | 250µg |
Source: | Pichia pastoris |
Mol. Wt: | 17-19 kD doublet |
Purification: | Purified from Pichia pastoris culture by HPLC gel filtration. Purity > 95 % by silver stained SDS-PAGE |
Concentration: | See product insert. |
Formulation: | Preservative-free and carrier-free in phosphate bufferedsaline, 360mM NaCl, pH 7.4. Sterile filtered. |
Storage: | Store at -20ºC. |
Notes: | (1) rAra h 2 has a C-terminal 6xHis-tag. (2) rAra h 2 appears as a doublet. (3) Avoid repeated Freeze/Thaw cycles. |
Genbank: | |
PDB: | |
Product Resources: | Recombinant Ara h 2 Certificate of Analysis |
Allergens are provided for research and commercial use in vitro: not for human in vivo or therapeutic use. | |
References: | |
1) Burks AW, Williams LW, Connaughton C, Cockrell G, O’Brien TJ, Helm RM. Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. J Allergy Clin Immunol 1992;90:962-9. 2) Sen M, Kopper R, Pons L, Abraham EC, Burks W, Bannon GA. Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-Binding epitopes. J Immunol 2002;169:882-7. 3) Flinterman AE, van Hoofen E, den Hartog Jager CF, Koppelman S, Pasmans SG, Hoekstra MO, Bruijnzeel-Koomen CA, Knulst AC, Knol EF. Children with peanut allergy recognize predominantly Ara h2 and Ara h 6, which remains stable over time. Clin Exp Allergy 2007;37:1221-8. 4) McDermott RA, Porterfield HS, El Mezayen R, Burks AW, Pons L, Schlichting DG, Solomon B, Redzic, JS, Harbeck RJ, Duncan MW, Hansen KC, Dreskin SC. Contribution of Ara h 2 to peanut-specific, immunoglobulin E-mediated, cell activation. Clin Exp Allergy 2007;37:752-763. |