Analytical Data
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Gene name
VTG2
- Application
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Alternative Names
Major vitellogeninVitellogenin II
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Species
Chicken
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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
P02845
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Expression Region
26-653aa
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Molecular Weight
74.9 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
VTG2, or vitellogenin 2, is a major yolk protein precursor found in various oviparous organisms, playing a crucial role in oocyte development and egg formation. Research on VTG2 has gained considerable attention due to its significance in reproductive biology and its potential applications in aquaculture and environmental monitoring. As a key component in the nutritional provisioning of developing embryos, VTG2 synthesis is tightly regulated by hormones such as estrogens, making it a valuable biomarker for assessing endocrine-disrupting chemicals in aquatic ecosystems. Furthermore, the study of VTG2 offers insights into evolutionary adaptations in reproductive strategies among different species, thus providing a comparative framework for understanding the molecular mechanisms underlying egg production. Advances in recombinant protein technologies have enabled the production of VTG2 in vitro, allowing for detailed investigations of its structure, function, and interactions with other molecular players during oogenesis. Overall, the exploration of VTG2 not only enhances our knowledge of reproductive physiology but also contributes to broader ecological and biotechnological applications, underscoring its significance in both basic and applied research contexts.
