Recombinant Fel d 1 Deglycosylated (RP-FD1D-1)

Purified from Pichia pastoris culture by  multi-step column chromatography. Purity on silver-stained SDS-PAGE >95%. 

See Product Insert. 

Preservative and carrier-free in phosphate buffered saline, pH 7.4. Filtered through 0.22µm filter.

1. N-glycosylation motif at position 103 was mutated (N103Q).
2. Upper band represents rFel d 1 dimer.
3. Fel d 1 chain 1 and chain 2 are fused by a 19 aa peptide linker (Ref.1).     
4. Avoid repeated Freeze/Thaw cycles

1. Vailes LD, Sun AW, Ichikawa K, Wu Z, Sulahian TH, Chapman MD, Guyre PM. High–level expression of immunoreactive recombinant cat allergen (Fel d 1):  Targeting to antigen-presenting cells.  J Allergy Clin Immunol 2002;110: 757-62.

2. Hulse KE, Reefer AJ, Engelhard VH, Satinover SM, Patrie JT, Chapman MD, Woodfolk JA. Targeting Fel d 1 to FcgRI induces a novel variation of the Th2 response in subjects with cat allergy. J Allergy Clin Immunol 2008. In press.

3. Kaiser L, Velickovic TC, Badia-Martinez D, Adedoyin J, Thunberg S, Hallén D, Berndt K, Grönlund H, Gafvelin G, van Hage M, Achour A. Structural characterization of the tetrameric form of the major cat allergen Fel d 1. J Mol Biol 2007; 370: 714-727.

4. Wünschmann S,  Vailes LD, King E, Albeerse RC, Chapman MD.  Expression of a Deglycosylated Recombinant Fel d 1 in Pichia pastoris. J Allergy Clin Immunol 2008; 121(2): S214