Analytical Data
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基因名
Pollen allergen Phl p 2
- Application
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别名
Allergen Phl p II Allergen: Phl p 2
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种属
Phleum pratense
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P43214
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表达区间
27-122aa
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分子量
26.8 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












