Analytical Data
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Gene name
GLT8D2
- Application
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Alternative Names
GLT8D2; GALA4A; UNQ1901/PRO4347; Glycosyltransferase 8 domain-containing protein 2; EC 2.4.1.-
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H1C3
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Expression Region
25-349aa
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Molecular Weight
41.2 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
GLT8D2, or glycosyltransferase 8 domain containing 2, is a member of the glycosyltransferase family, which is known to play critical roles in various biological processes, including cell signaling, protein stability, and immune responses. The study of GLT8D2 is particularly relevant due to its involvement in the synthesis of glycosylated molecules, which are essential for normal cellular function and communication. Recent research has suggested that GLT8D2 may be implicated in several diseases, including cancer, inflammatory conditions, and neurological disorders, making it a potential target for therapeutic interventions. The recombinant protein expression of GLT8D2 allows for in-depth structural and functional analyses, facilitating the understanding of its enzymatic mechanisms and biological functions. Researchers aim to elucidate the protein's role in glycosylation pathways and to explore how alterations in its expression levels might contribute to disease pathology. Furthermore, GLT8D2’s substrate specificity and interaction with other cellular components present exciting avenues for drug development and biotechnological applications. As such, the advancement of GLT8D2 recombinant protein studies represents a promising field of research with implications for both fundamental science and clinical applications.
