Recombinant Der p 1 deglycosylated (RP-DP1D-1)

Description
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Allergen:	rDer p 1 (Dermatophagoides pteronyssinus allergen 1) deglycosylated, house dust mite
Unit:	250µg
Source:	Pichia pastoris (clone N52Q, N-glycosylation site N52 mutated)
Mol. Wt:	24 kD
Purification:	Purified from Pichia pastoris culture by multi-step column chromatography. Purity on silver stained SDS-PAGE >95%.
Concentration:	See product insert.
Formulation:	Preservative and carrier-free in sterile, 0.1M CAPS Buffer, pH 9.5. Filtered through 0.22 µm filter.
Storage:	Store at -20ºC. Avoid freeze-thaw cycles.
Notes:	1. A LoTox™ product: Endotoxin ≤ 0.03 EU/µg. 2. Mature form of rDer p 1; proregion removed with acid dialysis. 3. Cysteine protease activity (DTT dependent): (see product insert) RFU @ 0.25µg/ml. 4. For stability purposes the product is shipped in CAPS Buffer pH9.5. It may be dialysed or diluted into a physiological buffer for cell culture purposes, but long term storage in PBS may cause precipitation.
Genbank:	U11695 = pro-Der p 1.0102 (difference is that in pro Der p 1.0105, V124 becomes A124)
PDB:	1XKG, 2AS8, 3F5V X-ray crystal structures
Product Resources:	Recombinant Der p 1 DG Certificate of Analysis
Allergens are provided for research and commercial use in vitro: not for human in vivo or therapeutic use.
References:
Hewitt CRA, Brown AP, Hart BJ, Pritchard DL. A major house dust mite allergen disrupts the Immunoglobulin E network by selectively cleaving CD23: innate protection by antiproteases. J Exp Med 1995;182:1537-1544. 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. 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. Best BE, Stedman KE, Bozic CM, Hunter SW, Vailes LD, Chapman MD, McCall CA, McDermott MJ. A recombinant group 1 house dust mite allergen, rDer f 1, with biological activities similar to those of the native allergen. Prot Exp Pur 2000;20:462-71. Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, Pomés A. Crystal structures 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.