Analytical Data
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Gene name
FGg
- Application
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Alternative Names
FG-G
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Species
Human
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Source
Yeast
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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
P02679
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Expression Region
Lys166~Asn416
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Molecular Weight
30kDa
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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
FGg recombinant protein research focuses on the development and application of a specific protein variant derived from the FGg gene, which encodes a glycoprotein known for its multifunctional roles in biological systems. The FGg protein has garnered attention due to its potential implications in various fields, including immunology, cancer therapy, and vaccine development. Understanding the structural and functional properties of FGg is crucial for elucidating its role in disease mechanisms, particularly in immune responses and tumor progression. The production of FGg as a recombinant protein allows for detailed studies of its biochemical characteristics and interactions with cellular receptors. Advances in recombinant DNA technology and protein expression systems have facilitated the large-scale synthesis of FGg, enabling researchers to explore its therapeutic potential. Investigations into FGg’s effects on cell signaling pathways and its ability to elicit immune responses are paving the way for innovative strategies in combating diseases. Additionally, the exploration of FGg's role in biomarker discovery and diagnostics further underscores its importance in translational research. Overall, the study of FGg recombinant protein serves as a vital area in modern biomedicine, promising new insights and applications in health science.
