Analytical Data
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Gene name
Pollen allergen Phl p 2
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简介
Pollen allergen Phl p 2 protein specifically expresses within pollen, intimately linked to plant reproductive structures and emphasizing its role in pollination processes. Pollen allergen Phl p 2 Protein, Phleum pratense (HEK293, His) is the recombinant Pollen allergen Phl p 2 protein, expressed by HEK293 , with N-6*His labeled tag. Pollen allergen Phl p 2 Protein, Phleum pratense (HEK293, His), has molecular weight of ~13.1 kDa.
- Application
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Alternative Names
Pollen allergen Phl p 2; PHLPII
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Species
Others
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Source
HEK293
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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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 2, derived from timothy grass (Phleum pratense), is a significant contributor to respiratory allergies, affecting millions of individuals worldwide. As a major allergen, Phl p 2 is known to trigger IgE-mediated responses, leading to symptoms such as allergic rhinitis and asthma. The increasing prevalence of pollen allergies has heightened the need for effective diagnosis and treatment strategies. Research on recombinant forms of Phl p 2 has become crucial, as these proteins can serve as valuable tools for allergen-specific immunotherapy and diagnostic applications. By utilizing recombinant technology, scientists can produce large quantities of purified allergens, enabling detailed studies of their structure, function, and immunological properties. Moreover, recombinant Phl p 2 can facilitate the development of hypoallergenic variants for potential therapeutic use, offering hope for improved patient management and quality of life for those affected by grass pollen allergies. Understanding the molecular mechanisms of Phl p 2 and its interaction with the immune system remains an active area of research, highlighting the importance of this allergen in the field of allergy immunology.
