Analytical Data
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Gene name
Vg
- Application
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Species
Honeybee
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q868N5
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Expression Region
1439-1672aa
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Molecular Weight
32.5 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
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.
