Analytical Data
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Gene name
POFUT2
- Application
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Alternative Names
GDP-fucose protein O-fucosyltransferase 2. EC:2.4.1.221. Peptide-O-fucosyltransferase 2. O-FucT-2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y2G5
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Expression Region
1-429 aa
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AA Sequence
MATLSFVFLLLGAVSWPPASASGQEFWPGQSAADILSGAASRRRYLLYDVNPPEGFNLRRDVYIRIASLLKTLLKTEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIEYEQFIAESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEFRSRHLNSTDDADRIPFQEDWMKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLMKTHRLDKVFVATDAVRKEYEELKKLLPEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACEQPTHWKITY
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Molecular Weight
76.4 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
POFUT2, or protein O-fucosyltransferase 2, is an enzyme that catalyzes the transfer of fucose, a sugar molecule, to specific serine and threonine residues on target proteins, primarily within the context of Notch signaling pathways. This O-fucosylation process is crucial for the proper functioning of various cellular processes, including cell differentiation, proliferation, and communication. Aberrant POFUT2 activity has been implicated in numerous diseases, including cancer, where altered glycosylation patterns can influence tumor growth and metastasis. Studies have shown that POFUT2 plays a pivotal role in regulating Notch receptor activation and modulating downstream signaling, which is essential for maintaining tissue homeostasis. Given the significance of glycosylation in protein function and the pathological consequences of its dysregulation, researchers have focused on characterizing POFUT2's structure and enzymatic mechanism, as well as exploring its potential as a therapeutic target. Understanding the nuances of POFUT2's activity could pave the way for novel interventions in diseases characterized by Notch signaling dysregulation, making it a key focus in the field of glycoscience and cancer research. Recent advances in recombinant protein technology have enabled the detailed study of POFUT2, providing insights into its substrate specificity and regulatory mechanisms, thereby enhancing our understanding of its biological roles and therapeutic potential.
