Analytical Data
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Gene name
GLT8D3
- Application
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Alternative Names
GXYLT1; GLT8D3; Glucoside xylosyltransferase 1; EC 2.4.2.42; Glycosyltransferase 8 domain-containing protein 3
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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
Q4G148
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Expression Region
1-409aa
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AA Sequence
MRRYLRVVVLCVACGFCSLLYAFSQLAVSLEEGTGGGGGKPQAAVASWLAGGGRGAVRGAGVAGPAAHPGVSDRYSLKIQPVEKMHLAVVACGERLEETMTMLKSAIIFSIKPLQFHIFAEDQLHHSFKGRLDNWSFLQTFNYTLYPITFPSENAAEWKKLFKPCASQRLFLPLILKEVDSLLYVDTDILFLRPVDDIWSLLKKFNSTQIAAMAPEHEEPRIGWYNRFARHPYYGKTGVNSGVMLMNMTRMRRKYFKNDMTTVRLQWGDILMPLLKKYKLNITWGDQDLLNIVFFHNPESLFVFPCQWNYRPDHCIYGSNCQEAEEGGIFILHGNRGVYHDDKQPAFRAVYEALRNCSFEDDNIRSLLKPLELELQKTVHTYCGKIYKIFIKQLAKSVRDRYARSPKEK
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Molecular Weight
73.2 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
GLT8D3 (Glycosyltransferase 8 Domain Containing 3) is a member of the glycosyltransferase family, playing a significant role in the biosynthesis of glycosylated molecules, which are crucial for various biological processes, including cell signaling, immune response, and pathogen interaction. Research into GLT8D3 has gained momentum in recent years due to its potential implications in cancer progression and neurodegenerative diseases. The enzyme's ability to modify glycan structures can influence cell surface properties and interactions, making it a target for therapeutic intervention. Additionally, GLT8D3 has been implicated in modulating the tumor microenvironment, affecting cancer cell proliferation and metastasis. Understanding the structure and function of recombinant GLT8D3 protein can provide insights into its enzymatic mechanisms and regulatory pathways. Moreover, studying this protein may reveal novel biomarkers for disease diagnosis or prognosis and contribute to the development of glycan-based therapies. Research efforts are focused on expressing and purifying GLT8D3 in various systems, characterizing its enzymatic activity, and exploring its interactions with other biomolecules. Overall, the investigation of GLT8D3 not only enhances our understanding of glycosylation processes but also opens new avenues for biotechnological applications and therapeutic strategies.
