Analytical Data
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Gene name
GCNT2
- Application
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Alternative Names
GCNT2; GCNT5; II; NACGT1; N-acetyllactosaminide beta-1.6-N-acetylglucosaminyl-transferase; N-acetylglucosaminyltransferase; EC 2.4.1.150; I-branching enzyme; IGNT
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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
Q8N0V5
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Expression Region
1-402aa
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AA Sequence
MNFWRYCFFAFTLLSVVIFVRFYSSQLSPPKSYEKLNSSSERYFRKTACNHALEKMPVFLWENILPSPLRSVPCKDYLTQNHYITSPLSEEEAAFPLAYVMVIHKDFDTFERLFRAIYMPQNVYCVHVDEKAPAEYKESVRQLLSCFQNAFIASKTESVVYAGISRLQADLNCLKDLVASEVPWKYVINTCGQDFPLKTNREIVQHLKGFKGKNITPGVLPPDHAIKRTKYVHQEHTDKGGFFVKNTNILKTSPPHQLTIYFGTAYVALTRDFVDFVLRDQRAIDLLQWSKDTYSPDEHFWVTLNRVSGVPGSMPNASWTGNLRAIKWSDMEDRHGGCHGHYVHGICIYGNGDLKWLVNSPSLFANKFELNTYPLTVECLELRHRERTLNQSETAIQPSWYF
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Molecular Weight
72.9 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
GCNT2, or GlcNAc transferase 2, plays a crucial role in glycosylation, specifically in the biosynthesis of complex N-glycans and O-glycans. It is essential for the development of various tissues and organs, influencing cell signaling, adhesion, and immune responses. Aberrant GCNT2 activity has been linked to several diseases, including cancer, diabetes, and inflammatory disorders. Its function is particularly significant in the context of tumor biology, as altered glycosylation patterns can affect tumor progression and metastasis. The recombinant expression of GCNT2 is vital for studying its enzymatic properties, substrate specificity, and regulatory mechanisms. By producing and characterizing GCNT2 as a recombinant protein, researchers aim to elucidate its role in glycan biosynthesis and its implications in health and disease. This understanding could lead to novel therapeutic strategies targeting glycosylation pathways, offering potential interventions in pathological conditions associated with GCNT2 dysregulation.
