Analytical Data
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Gene name
RFNG
- Application
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Alternative Names
RFNG；Beta-1.3-N-acetylglucosaminyltransferase radical fringe
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y644
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Expression Region
1-331aa
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AA Sequence
MSRARGALCRACLALAAALAALLLLPLPLPRAPAPARTPAPAPRAPPSRPAAPSLRPDDVFIAVKTTRKNHGPRLRLLLRTWISRARQQTFIFTDGDDPELELQGGDRVINTNCSAVRTRQALCCKMSVEYDKFIESGRKWFCHVDDDNYVNARSLLHLLSSFSPSQDVYLGRPSLDHPIEATERVQGGRTVTTVKFWFATGGAGFCLSRGLALKMSPWASLGSFMSTAEQVRLPDDCTVGYIVEGLLGARLLHSPLFHSHLENLQRLPPDTLLQQVTLSHGGPENPHNVVNVAGGFSLHQDPTRFKSIHCLLYPDTDWCPRQKQGAPTSR
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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 (Ridge Factor N-Glycosylation) is a highly conserved glycosyltransferase that plays a critical role in modifying proteins through the addition of specific carbohydrate moieties. This modification is essential for various physiological processes, including cellular communication, immune response, and developmental regulation. Recent studies have highlighted RFNG’s involvement in the Notch signaling pathway, which is crucial for cell differentiation and tissue development. Aberrant RFNG activity has been linked to several diseases, including cancer, where it may influence tumor progression and metastasis by modulating Notch signaling and enhancing the glycosylation of tumor-associated antigens. To understand the functional implications of RFNG in these biological pathways, researchers have focused on the recombinant expression and purification of RFNG proteins. This enables detailed biochemical characterization, structure-function studies, and exploration of the enzyme's glycosylation patterns. Advances in recombinant DNA technology and protein engineering have facilitated the production of RFNG variants with altered enzymatic properties, providing insights into the relationship between RFNG's structure and its biological functions. Understanding RFNG's role at the molecular level is not only pivotal for unraveling its contributions to normal physiology but also holds promise for the development of novel therapeutic strategies targeting RFNG in disease contexts.
