Analytical Data
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Gene name
Der p 23
- Application
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Alternative Names
Major house dust mite allergen Der p 23 （Major HDM allergen Der p 23） (Peritrophin-like protein Der p 23)
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Species
Dermatophagoides pteronyssinus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
L7N6F8
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Expression Region
22-90aa
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Molecular Weight
13.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Der p 23 is a major allergen derived from the house dust mite Dermatophagoides pteronyssinus, known for its significant role in triggering allergic reactions and asthma in sensitized individuals. As a highly prevalent source of indoor allergens, Der p 23 has garnered considerable attention in allergy research. The recombinant form of this allergen allows for a deeper understanding of its immunological properties, facilitating the development of targeted diagnostic tools and therapeutic interventions. Studies involving Der p 23 have demonstrated its ability to elicit strong IgE antibody responses, which are critical in the pathogenesis of allergic diseases. Additionally, research has focused on the protein's structural characteristics, revealing how specific epitopes interact with IgE and contribute to allergic sensitization. Understanding these mechanisms is vital for designing allergen-specific immunotherapies, potentially leading to better management strategies for allergic diseases. Moreover, advancements in recombinant technology have enabled the production of Der p 23 in a controlled environment, reducing the risk of contamination and variability associated with natural sources, and providing a valuable resource for clinical and experimental studies. Overall, the investigation of Der p 23 as a recombinant protein plays a pivotal role in elucidating the underlying mechanisms of allergenicity and in improving allergy diagnostics and treatments.
