Analytical Data
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Gene name
FIGN
- Application
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Species
Human
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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
Q5HY92
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Expression Region
Met1~Leu308
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Molecular Weight
41kDa
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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
FIGN protein, or Fignin, has garnered attention in the field of molecular biology due to its potential role in various physiological processes and its implications in disease mechanisms. Initial studies suggest that FIGN is involved in key cellular functions such as signal transduction, protein-protein interactions, and the regulation of gene expression. These functions point to its potential importance in developmental biology and in the context of human health and disease. Researchers have identified that alterations in FIGN expression or function may be linked to various pathologies, including cancer and neurodegenerative disorders. The recombinant production of FIGN protein allows for in-depth investigation into its structure-function relationship, enzymatic activity, and interaction with other biomolecules. Studying FIGN's recombinant form aids in elucidating its biological role and therapeutic potential. As a result, understanding FIGN through recombinant technology could pave the way for novel therapeutic strategies and biomarkers, enhancing our grasp of complex diseases and their treatments. This burgeoning area of research highlights the need for comprehensive functional studies, structural analyses, and in vivo investigations to fully decode the role of FIGN in health and disease.
