Analytical Data
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Gene name
DERP5
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简介
DERP5 protein exhibits a monomeric structure and forms homodimeric trimers through concentration-dependent oligomerization, which plays a key role in allergic reactions. Multiple population studies have shown that DERP5 binds to IgE and is associated with mite allergy symptoms such as asthma and rhinitis. DERP5 Protein, Dermatophagoides pteronyssinus (His) is the recombinant DERP5 protein, expressed by E. coli , with N-His labeled tag.
- Application
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Alternative Names
Mite allergen Der p 5; Allergen Der p V; IgE-binding allergen; Der p 5
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Species
Others
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14004
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Expression Region
M1-V132
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Protein Length
Full Length
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Molecular Weight
15 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
Related Products
Protein Description
DERP5, or Defensin-related protein 5, is a member of the defensin family known for its antimicrobial properties, predominantly expressed in the respiratory and reproductive tissues of various species. Its role has garnered significant interest due to its potential involvement in innate immunity, where it might contribute to the host defense against pathogens. Studies have indicated that DERP5 exhibits unique structural features that may enhance its functional attributes, prompting researchers to investigate its biophysical properties and possible therapeutic applications. Understanding the expression regulation of DERP5 in response to infections or inflammatory stimuli is crucial, as it could lead to new insights into disease mechanisms and the development of novel interventions. Additionally, the recombinant production of DERP5 facilitates detailed studies on its structure-function relationship, enabling exploration of its potential as a biomarker or a therapeutic agent in enhancing immune responses. As research progresses, DERP5 may play a pivotal role in advancing our knowledge of antimicrobial peptides and their applications in medical science.
