Analytical Data
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Gene name
GCNT3
- Application
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Alternative Names
GCNT3; Beta-1.3-galactosyl-O-glycosyl-glycoprotein beta-1.6-N-acetylglucosaminyltransferase 3; C2GnT-mucin type; C2GnT-M; hC2GnT-M; Core 2/core 4 beta-1.6-N-acetylglucosaminyltransferase; C2/4GnT
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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
O95395
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Expression Region
28-126aa
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AA Sequence
KLSFRLKCDSDHLGLESRESQSQYCRNILYNFLKLPAKRSINCSGVTRGDQEAVLQAILNNLEVKKKREPFTDTHYLSLTRDCEHFKAERKFIQFPLSK
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Molecular Weight
36.63 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
Related Products
Protein Description
GCNT3 (Group 3 Glycosyltransferase 6) is a member of the glycosyltransferase family that plays a critical role in the biosynthesis of glycoproteins and glycolipids, influencing various biological processes such as cell adhesion, signaling, and immune response. The enzyme specifically catalyzes the addition of glycan structures to the antigen Kamino to form the Lewis X structure, which is vital for cell-cell interactions and recognition in physiological and pathological contexts. Aberrant expression of GCNT3 has been associated with several diseases, including cancer, where altered glycosylation patterns can contribute to tumor progression and metastasis. Understanding the biochemical properties and functional implications of GCNT3 is crucial for revealing its potential as a biomarker or therapeutic target. Recombinant GCNT3 protein can be produced to facilitate detailed studies of its enzymatic activity, substrate specificity, and interaction with other cellular components. This research aims to elucidate the molecular mechanisms underlying its role in glycosylation pathways and their impact on cellular behavior, thus contributing to the broader field of glycobiology and its application in disease diagnosis and treatment strategies.
