Analytical Data
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Gene name
GAL3ST3
- Application
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Alternative Names
GAL3ST3；Galactose-3-O-sulfotransferase 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
SWYPKLFPLSCPPLRNSPPRPKHMTVAFLKTHKTAGTTVQNILFRFAERHNLTVALPHPSCEHQFCYPRNFSAHFVHPATRPPHVLASHLRFDRAELERLMPPSTVYVTILREPAAMFESLFSYYNQYCPAFRRVPNASLEAFLRAPEAYYRAGEHFAMFAHNTLAYDLGGDNERSPRDDAAYLAGLIRQVEEVFSLVMIAEYFDESLVLLRRLLAWDLDDVLYAKLNARAASSRLAAIPAALARAARTWNALDAGLYDHFNATFWRHVARAGRACVEREARELREARQRLLRRCFGDEPLLRPAAQIRTKQLQPWQPSRKVDIMGYDLPGGGAGPATEACLKLAMPEVQYSNYLLRKQKRRGGARARPEPVLDNPPPRPIRVLPRGPQGP
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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, or Galactosyltransferase 3, is an enzyme that plays a crucial role in the biosynthesis of glycosaminoglycans, specifically in the sulfation of galactose residues in proteoglycans. These proteoglycans are vital for various biological processes, including cell signaling, development, and tissue repair. A growing body of research has implicated GAL3ST3 in several pathological conditions, including cancer and cardiovascular diseases, due to its influence on cellular environments and interactions. Understanding the structure-function relationship of GAL3ST3 can provide insights into its role in these diseases, offering potential for targeted therapeutic strategies. The recombinant production of GAL3ST3 in laboratory settings allows for detailed characterization of its enzymatic properties, substrate specificity, and regulatory mechanisms. Such studies often utilize various expression systems, including bacterial and mammalian cells, to achieve high yields of functional protein. The insights gained from GAL3ST3 research could illuminate new avenues in drug development and enhance our comprehension of glycosylation processes in health and disease. Overall, the study of GAL3ST3 and its recombinant protein offers significant promise for advancing biochemical knowledge and therapeutic applications in the context of glycosylation dynamics.
