Analytical Data
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Gene name
MALD3
- Application
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Alternative Names
Allergen: Mal d 3
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Species
Malus domestica
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9M5X7
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Expression Region
25-115aa
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Molecular Weight
25.1 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
MALD3 (MALD-3) is a recombinant protein that has gained attention in the fields of immunology and biotechnology due to its potential applications in vaccine development and therapeutic interventions. As a member of the Mal d 3 protein family, which is predominantly found in apple, MALD3 is known to be a significant allergen responsible for apple allergies in sensitive individuals. The study of MALD3 is crucial for understanding the molecular mechanisms underlying allergic reactions and for developing hypoallergenic apple varieties through recombinant DNA technology. Furthermore, researchers are investigating the structural and functional properties of MALD3 to explore its role in eliciting immune responses, potentially paving the way for novel immunotherapy strategies. As food allergies continue to rise globally, the characterization of MALD3 could lead to better diagnostic methods and improved food safety measures, ultimately benefiting patients and healthcare professionals alike. This research not only contributes to the fundamental understanding of allergenic proteins but also highlights the importance of interdisciplinary approaches in tackling modern health challenges.
