Analytical Data
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Gene name
Pollen allergen Phl p 5b
- Application
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Alternative Names
Allergen Phl p Va Allergen: Phl p 5a
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Species
Phleum pratense
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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
Q40962
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Expression Region
1-286aa
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Molecular Weight
44.5 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
Pollen allergen Phl p 5b, a significant allergen derived from Timothy grass (Phleum pratense), has garnered substantial attention in the field of allergy research due to its role in inducing allergic responses in sensitized individuals. Grass pollen allergy is a prevalent condition that affects millions, leading to symptoms such as rhinitis, asthma, and overall diminished quality of life during peak pollen seasons. The Phl p 5b protein is part of a group of non-specific lipid transfer proteins (nsLTPs) known for their capacity to trigger IgE-mediated allergic reactions. Understanding the structure and function of Phl p 5b is crucial for developing effective diagnostic and therapeutic strategies, including allergen immunotherapy. Recent advancements in recombinant DNA technology have facilitated the production of this allergen in a lab setting, allowing researchers to study its properties without the variability associated with natural sources. This recombinant protein serves as a valuable tool for investigating allergenicity, assessing immune responses, and screening potential treatments. Characterizing Phl p 5b at the molecular level also contributes to the overall understanding of cross-reactivity among various pollen allergens, aiding in the development of more targeted and personalized therapeutic approaches for those affected by grass pollen allergies. The ongoing research into recombinant Phl p 5b not only holds promise for improved allergy management but also enhances our knowledge of allergic mechanisms, ultimately contributing to the broader field of immunology and allergy treatment.
