Recombinant Ara h 2 (RP-AH2-1)

rAra h 2.0201 (Arachis hypogaea allergen 2), peanut

Glycosylation site N127 mutated (N127Q

Purified from Pichia pastoris culture by multi-step HPLC. 

Purity > 95 % by silver stained SDS-PAGE

See product insert. 

Preservative-free and carrier-free in phosphate buffered saline, 360mM NaCl, pH 7.4. Sterile filtered. 

(1) rAra h 2 has a C-terminal 6xHis-tag.

(2) rAra h 2 appears as a doublet.

(3) Avoid repeated Freeze/Thaw cycles.

Recombinant Ara h 2 Certificate of Analysis

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.