Analytical Data
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Gene name
GCNT1
- Application
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Alternative Names
GCNT1. NACGT2
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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
Q02742
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Expression Region
1-428aa
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AA Sequence
MLRTLLRRRLFSYPTKYYFMVLVLSLITFSVLRIHQKPEFVSVRHLELAGENPSSDINCTKVLQGDVNEIQKVKLEILTVKFKKRPRWTPDDYINMTSDCSSFIKRRKYIVEPLSKEEAEFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDTKSEDSYLAAVMGIASCFSNVFVASRLESVVYASWSRVQADLNCMKDLYAMSANWKYLINLCGMDFPIKTNLEIVRKLKLLMGENNLETERMPSHKEERWKKRYEVVNGKLTNTGTVKMLPPLETPLFSGSAYFVVSREYVGYVLQNEKIQKLMEWAQDTYSPDEYLWATIQRIPEVPGSLPASHKYDLSDMQAVARFVKWQYFEGDVSKGAPYPPCDGVHVRSVCIFGAGDLNWMLRKHHLFANKFDVDVDLFAIQCLDEHLRHKALETLKH
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Molecular Weight
76.2 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
Related Products
Protein Description
GCNT1 (Glycosyltransferase 1, Galactosyltransferase) is an enzyme that plays a crucial role in the biosynthesis of glycoproteins and glycolipids by adding galactose to specific glycans. The study of recombinant GCNT1 protein has garnered significant attention due to its implications in various biological processes, including cell signaling, immune response, and pathogen recognition. Abnormal expression or mutations of GCNT1 have been linked to several diseases, particularly in the context of cancer, where altered glycosylation patterns can affect tumor progression and metastasis. Furthermore, GCNT1 is essential for the synthesis of certain carbohydrate structures that are vital for cellular interactions and stability. The production of recombinant GCNT1 allows researchers to investigate its enzymatic properties, substrate specificity, and regulatory mechanisms in detail, facilitating a deeper understanding of its functional roles in health and disease. By utilizing advanced molecular biology techniques, including gene cloning and expression systems, scientists can produce GCNT1 in sufficient quantities for biochemical characterization and potential therapeutic applications. Understanding the structure-function relationship of GCNT1 through recombinant protein studies may ultimately pave the way for developing novel glycan-based diagnostics and therapeutics, highlighting the importance of this glycosyltransferase in modern biomedical research.
