Analytical Data
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Gene name
GAL3ST3
- Application
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Alternative Names
Galactose-3-O-sulfotransferase 3(Gal3ST-3)(EC 2.8.2.-)(Beta-galactose-3-O-sulfotransferase 3)(Gal3ST3)(Gal-beta-1, 3-GalNAc 3'-sulfotransferase 3)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96A11
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Expression Region
41-431aa
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Molecular Weight
51.9 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
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Protein Description
GAL3ST3 (Galactose-3-O-sulfotransferase 3) is a key enzyme involved in the sulfation of glycosaminoglycans, particularly heparan sulfate and keratan sulfate, which play crucial roles in various biological processes, including cell signaling, development, and tissue repair. The study of GAL3ST3 is particularly relevant due to its implications in several pathophysiological conditions, such as cancer progression and cardiovascular diseases. Understanding its biochemical properties and regulatory mechanisms can provide significant insights into its function in health and disease. Recombination technology allows for the production of GAL3ST3 recombinant proteins, enabling researchers to investigate its enzymatic activity and substrate specificity in controlled laboratory environments. By generating and characterizing these recombinant proteins, scientists can explore the structural attributes that influence the enzyme's function and its interactions with various ligands. This research is critical for developing targeted therapeutic strategies that modulate sulfation processes, potentially offering new avenues for treating diseases associated with aberrant glycosaminoglycan sulfation. Furthermore, recombinant GAL3ST3 may serve as a valuable tool for high-throughput screening and the discovery of small molecule inhibitors, enhancing our understanding of glycan biology and its therapeutic potential.
