From delipidated peanut extract by multi-step chromatography.

Purity on silver stained SDS-PAGE >95%.

See product insert.

Preservative and carrier-free in sterile, endotoxin-free,

phosphate buffered saline, pH 7.4

(1) Ara h 2 appears as a doublet (4).

(2) Avoid repeated Freeze/Thaw cycles.

(3) A LoTox™ product, Endotoxin < 0.01 EU/μg.

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.