关键信息
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基因名
Vg
- 应用
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种属
Honeybee
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q868N5
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表达区间
1439-1672aa
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分子量
32.5 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.
质检流程
相关产品
背景信息
The study of Vg (vitellogenin) recombinant proteins is rooted in the broader context of understanding reproductive biology and its applications in biotechnology and environmental monitoring. Vitellogenin is a precursor protein synthesized in response to estrogen and is vital for oogenesis in oviparous organisms, primarily in fish and amphibians. Its production reflects the hormonal status and reproductive health of these species. Research on recombinant Vg proteins allows scientists to explore molecular mechanisms behind reproductive processes, assess the impacts of endocrine-disrupting chemicals in aquatic ecosystems, and develop tools for bioindicators of environmental pollution. Additionally, Vg proteins have potential applications in biopharmaceuticals, as they can be engineered to facilitate the delivery of therapeutic agents. The ability to produce Vg in a recombinant form enhances its availability for various experimental purposes, including functional assays and structural studies, further driving advancements in comparative physiology and toxicology. Understanding the characteristics and functions of Vg and its recombinant variants is crucial for developing strategies to monitor environmental health and protect biodiversity, making it a significant focus in both basic and applied research.
