Analytical Data
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Gene name
LFNG
- Application
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Alternative Names
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NES3
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Expression Region
1-250aa
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Molecular Weight
55.2 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
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Protein Description
LFNG (Lunatic Fringe) is a notable member of the Fringe family of glycosyltransferases, which play a critical role in the Notch signaling pathway, a fundamental mechanism for cell communication and differentiation in various biological processes, including embryogenesis and tissue homeostasis. The modification of Notch ligands by LFNG is essential for regulating the interaction between Notch receptors and their ligands, thus modulating cell fate decisions. Given its pivotal role in developmental biology and potential implications in diseases such as cancer, neurodegeneration, and other disorders influenced by aberrant Notch signaling, LFNG has garnered significant research interest. Studies have demonstrated that LFNG not only affects cell proliferation and differentiation but also participates in the regulation of stem cell populations and organ development. Moreover, understanding LFNG's structure and function is paramount for developing targeted therapies that can manipulate Notch signaling in various pathologies. Researchers have embarked on characterizing the recombinant LFNG protein to elucidate its enzymatic activity, substrate specificity, and overall impact on signaling pathways. Investigations into LFNG's crystal structure and its interaction with glycoproteins are crucial for designing small molecules or biologics that could selectively modulate LFNG's activity, presenting new avenues for therapeutic intervention in Notch-related diseases.
