LoTox™ D. pteronyssinus Antigen (LTN-DPE-1)

Description
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Allergen:	Dermatophagoides pteronyssinus, house dust mite
Source:	D.pteronyssinus spent mite culture
Mol. Wt:	Der p 1: 24kD and Der p 2: 14kD
ELISA	See product insert (defined amounts of Der p 1 and Der p 2)
Concentration:	See product insert.
Volume	1 ml
Formulation:	Preservative and carrier-free in sterile, endotoxin-free, phosphate buffered saline, pH 7.4. Sterile filtered.
Storage:	Store at -20ºC. Do not allow product to remain at 4°C or room temperature for extended periods of time. Refreeze unused portion and aliquot into smaller quantities if necessary to avoid freeze/thaw cycles.
Notes	A LoToxTM product: Endotoxin ≤ 0.03 EU/µg. Cysteine protease activity: See product insert. Serine protease activity: See product insert. Use sterile tips to avoid contamination of product.
PDB:
Product Resources:	LoTox™ D. pteronyssinus Antigen Certificate of Analysis
Allergens are provided for research and commercial use in vitro: not for human in vivo or therapeutic use.
References:
Lombardero M, Heymann PW, Platts-Mills TAE, Fox JW, Chapman MD. Conformational stability of B cell epitopes on Group 1 and Group II Dermatophagoides spp. Allergens. Effect of thermal and chemical denaturation on the binding of murine IgG and human IgE antibodies. J Immunol 1990;144:1353-1360. Schultz O, Laing P, Sewell HF, Shakib F. Der p 1, a major allergen of the house dust mite, proteolytically cleaves the low affinity receptor for human IgE (CD23). Eur J Immunol 1995;25:3191-3194. King C, Brennan S, Thompson PJ, Stewart GA. Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium. J Immunol 1998; 161:3645-3651. Gough L, Schultz O, Sewell HF, Shakib F. The cysteine protease activity of the major house dust mite allergen Der p 1 selectively enhances the immunoglobulin E antibody responses. J Exp Med 1999; 190:1897-1901. Wan H, Winton HL, Soeller C, Tovey ER, Gruenert DC, Thompson PJ, Stewart GA, Taylor GW, Garrod DR, Cannell MD, Robinson C. Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions. J Clin Invest 1999; 104:123-133. Trompette A, Divanovic S, Visintin A, Blanchard C, Hegde RS, Madan R, Thorne PS, Wills-Karp M, Gioannini TL, Weiss JP, Karp CL. Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein. Nature 2008, Dec. 7. Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, Pomés A. Crystal structure of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding. J Mol Biol, 2009;386:520-530.