The E.Coli derived recombinant protein contains the Dermatophagoides pteronyssinus Dust Mite Der P1 protein (a.a. 20-320) and fused to a 6 His Tag at C-terminus, having a total Mw of 34.5kDa, pI 5.6.
Purified by proprietary chromatographic technique.
Der P1 is a thiol protease with a preference for substrates that have a large hydrophobic side chain in the P2 position or basic residues . It is a member of the C1 peptidase family and exhibits extensive endopeptidase specificity . The protein is also N-glycosylated, meaning it has carbohydrate groups attached to it, which can affect its function and allergenicity .
Der P1 is highly allergenic and is one of the primary causes of perennial asthma worldwide . Chronic exposure to Der P1 occurs through inhalation, leading to the production of IgE antibodies in susceptible individuals . The allergenicity of Der P1 is partly due to its ability to cleave various receptors on human cells, such as the CD23 receptor on B cells and the IL-2 receptor on T cells .
Research on Der P1 has provided detailed insights into the interactions between this allergen and antibodies. For example, structural analyses have revealed the epitopes (specific parts of the allergen that antibodies bind to) and how these interactions contribute to the allergenicity of Der P1 . This information is valuable for designing immunotherapies that can reduce the binding of antibodies to Der P1, potentially alleviating allergic reactions .