Analytical Data
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Gene name
EXT1
- Application
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Alternative Names
EXT; Ttv; LGCR, LGS; Langer-Giedion Syndrome Chromosome Region; Glucuronosyl-N-acetylglucosaminyl-Proteoglycan 4-Alpha-N-Acetylglucosaminyltransferase
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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
Q16394
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Expression Region
Cys334~Arg549
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Molecular Weight
27kDa
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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
EXT1, or exostosin glycosyltransferase 1, is a critical enzyme involved in the biosynthesis of heparan sulfate, a polysaccharide that plays key roles in numerous biological processes, including cell signaling, tissue development, and repair. Mutations in the EXT1 gene are associated with multiple osteochondromas, a hereditary condition characterized by the formation of benign bone tumors. Research on EXT1 recombinant proteins has gained momentum, given its implications in tumorigenesis and potential therapeutic targets. By expressing and purifying EXT1 in a heterologous system, researchers aim to better understand its enzymatic mechanisms and structural characteristics. Such studies provide insights into the role of heparan sulfate in cancer biology, as well as the enzyme's function in other physiological contexts. The recombinant EXT1 can also serve as a platform for drug design, revealing potential inhibitors that could modulate its activity, offering new avenues for treatment. Overall, the investigation of EXT1 not only enhances our understanding of the molecular basis of related diseases but also holds promise for the development of novel therapeutic strategies.
