Analytical Data
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Gene name
Vg
- Application
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Alternative Names
Vg；VGR；Bone morphogenetic Protein 6
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22004
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Expression Region
382-513aa
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AA Sequence
QQSRNRSTQSQDVARVSSASDYNSSELKTACRKHELYVSFQDLGWQDWIIAPKGYAANYCDGECSFPLNAHMNATNHAIVQTLVHLMNPEYVPKPCCAPTKLNAISVLYFDDNSNVILKKYRNMVVRACGCH
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Molecular Weight
18.9kDa
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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 has gained significant attention due to their crucial role in various biological processes, particularly in reproduction and development in many organisms. Vitellogenin is a precursor of egg yolk proteins, synthesized in the liver of female oviparous animals, and plays a vital role in oogenesis by providing essential nutrients to the developing embryos. Research on Vg has expanded beyond traditional studies of reproductive biology, as Vg is now recognized as a biomarker for environmental stress and endocrine disruption in aquatic systems. The recombinant production of Vg proteins allows for the study of their structure-function relationships, providing insights into how these proteins interact with other molecules and their roles in cellular processes. Furthermore, recombinant Vg can facilitate the development of novel biotechnological applications, including its use in aquaculture and as a tool in ecotoxicological assessments. As the understanding of Vg’s multifaceted functions continues to evolve, the ability to produce and manipulate recombinant Vg proteins opens up new avenues for research in developmental biology, environmental science, and biotechnology. This growing body of knowledge not only enhances our understanding of reproductive mechanisms but also aids in assessing the impacts of pollutants on wildlife, thereby contributing to conservation efforts and sustainable practices in managing aquatic ecosystems.
