Analytical Data
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Gene name
LFNG
- Application
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Alternative Names
LFNG；Beta-1.3-N-acetylglucosaminyltransferase lunatic 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
Q8NES3
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Expression Region
1-250aa
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AA Sequence
MTPGRCCLAADIQVETFIFTDGEDEALARHTGNVVITNCSAAHSRQALSCKMAVEYDRFIESGRKWFCHVDDDNYVNLRALLRLLASYPHTRDVYVGKPSLDRPIQAMERVSENKVRPVHFWFATGGAGFCISRGLALKMSPWASGGHFMNTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTSELHEQVTLSYGMFENKRNAVHVKGPFSVEADPSRFRSIHCHLYPDTPWCPRTAIF
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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 member of the Rous-Sarcoma virus (RSV) glycoprotein family and plays a crucial role in the Notch signaling pathway, which is essential for various developmental processes and cellular differentiation. The study of LFNG has garnered attention due to its involvement in modulating cell fate decisions during embryonic development, as well as its implications in pathologies such as cancer and congenital disorders. Research indicates that LFNG acts as a glycosyltransferase that adds fucose to specific Notch ligands, altering their interaction with Notch receptors. This post-translational modification is critical for controlling signal transduction within the Notch pathway, influencing cellular behaviors like proliferation, apoptosis, and differentiation. The understanding of LFNG's function and its regulatory mechanisms provides insights into how disrupted Notch signaling contributes to diseases, making LFNG a potential therapeutic target. Recent advancements in recombinant protein production techniques have facilitated the study of LFNG, allowing researchers to investigate its structural properties, enzymatic activity, and interaction profiles in vitro and in vivo. As researchers continue to explore the multifaceted roles of LFNG in development and disease, its potential as a biomarker or therapeutic target remains a forefront area of research in molecular biology and medicinal chemistry.
