Analytical Data
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Gene name
RFNG
- Application
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Alternative Names
Radical Fringe Homolog; Beta-1,3-N-acetylglucosaminyltransferase radical fringe
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Species
Rat
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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
Q6P6T7
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Expression Region
Lys68~Val312
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Molecular Weight
31kDa
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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
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Protein Description
RFNG (Rounding-Factor-Related Gene) is a crucial protein involved in the regulation of glycans during cellular processes, particularly in the Notch signaling pathway. This pathway is essential for various developmental and biological functions, including cell differentiation and proliferation. Aberrations in Notch signaling have been associated with numerous diseases, such as cancer and developmental disorders. Given its significant role, RFNG has garnered attention in the field of molecular biology and biochemistry. Researchers have focused on characterizing the structure and function of RFNG to better understand its mechanism of action and its impact on cellular communication. The recombinant expression of RFNG in various systems, such as E. coli or mammalian cells, allows for detailed studies of its enzymatic activity and interactions with other proteins involved in glycosylation. Understanding RFNG's functionality may provide insights into therapeutic interventions targeting Notch-related diseases. Additionally, the study of RFNG and its glycan modifications can offer potential biomarkers for disease progression, further emphasizing the protein's importance in clinical research. Overall, the ongoing investigation into RFNG's role in glycosylation and cellular signaling underscores the need for comprehensive studies that could ultimately lead to novel therapeutic strategies and a deeper understanding of complex biological networks.
