Analytical Data
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Gene name
Furin/PCSK3
- Application
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Alternative Names
Short name: Ferric uptake regulator
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Species
Escherichia coli
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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
P0A9A9
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Expression Region
2-148aa
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Molecular Weight
20.7 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
Furin, also known as PCSK3 (Proprotein Convertase Subtilisin/Kexin type 3), is a member of the proprotein convertase family, which plays a crucial role in the proteolytic processing of various precursor proteins, influencing a wide range of biological processes such as cell signaling, metabolism, and tissue homeostasis. It is primarily localized in the trans-Golgi network and is involved in the activation of several proproteins, including hormones, neuropeptides, and viral glycoproteins. Dysregulation of Furin/PCSK3 activity has been linked to numerous diseases, including cancer, cardiovascular disorders, and viral infections, making it an attractive target for biomedical research. The generation of recombinant Furin/PCSK3 proteins has facilitated in-depth studies of its enzymatic mechanisms, substrate specificity, and regulatory roles in cellular processes. Advanced techniques such as X-ray crystallography and cryo-electron microscopy have provided insights into its structural properties, aiding in the design of specific inhibitors. Furthermore, understanding the dynamics of Furin/PCSK3 has implications for therapeutic interventions, including the development of drugs that can modulate its activity for treating diseases associated with its misregulation. This research is particularly significant in the context of emerging infectious diseases, where Furin’s role in viral maturation and entry highlights its relevance in developing antiviral strategies. Overall, Furin/PCSK3 remains a vital subject of study within biochemistry and molecular biology, with promising prospects for therapeutic applications in various health conditions.
