Analytical Data
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Gene name
Ara h 1
- Application
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Alternative Names
Allergen Ara h I
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Species
Arachis hypogaea
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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
P43237
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Expression Region
26-614aa
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Molecular Weight
71.7 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
Ara h 1 is a key allergenic protein found in peanuts, primarily responsible for inducing allergic reactions in sensitized individuals. The prevalence of peanut allergies has been on the rise in recent decades, affecting millions worldwide and posing significant health risks, particularly in children. Research into Ara h 1 is crucial for understanding the molecular mechanisms underlying these allergic responses. This protein belongs to the cupin superfamily and typically exists in a dimeric form, which contributes to its stability and allergenic potential. Studies have shown that Ara h 1 can elicit strong IgE-mediated immune responses, leading to symptoms ranging from mild oral allergy syndrome to severe anaphylaxis. In recent years, the focus has shifted towards the recombinant expression of Ara h 1 to facilitate the development of diagnostic tools and therapeutic strategies, including desensitization therapies. By using recombinant DNA technology, researchers can produce a more uniform and safer form of the protein for research and clinical applications. Understanding the structure-function relationship of Ara h 1 and its interaction with the immune system is critical not only for advancing peanut allergy research but also for creating targeted interventions to reduce allergic reactions. Moreover, the insights gained from Ara h 1 studies could pave the way for broader applications in allergen management and prevention strategies, ultimately improving the quality of life for individuals affected by this common food allergy. Continued research into Ara h 1 and its implications holds promise for innovative approaches to allergy diagnosis and treatment, contributing to a better understanding of food allergies at large.
