Analytical Data
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Gene name
ALG6
- Application
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Alternative Names
ALG6; My046; Dolichyl pyrophosphate Man9GlcNAc2 alpha-1.3-glucosyltransferase
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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
Q9Y672
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Expression Region
1-507aa
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AA Sequence
MEKWYLMTVVVLIGLTVRWTVSLNSYSGAGKPPMFGDYEAQRHWQEITFNLPVKQWYFNSSDNNLQYWGLDYPPLTAYHSLLCAYVAKFINPDWIALHTSRGYESQAHKLFMRTTVLIADLLIYIPAVVLYCCCLKEISTKKKIANALCILLYPGLILIDYGHFQYNSVSLGFALWGVLGISCDCDLLGSLAFCLAINYKQMELYHALPFFCFLLGKCFKKGLKGKGFVLLVKLACIVVASFVLCWLPFFTEREQTLQVLRRLFPVDRGLFEDKVANIWCSFNVFLKIKDILPRHIQLIMSFCSTFLSLLPACIKLILQPSSKGFKFTLVSCALSFFLFSFQVHEKSILLVSLPVCLVLSEIPFMSTWFLLVSTFSMLPLLLKDELLMPSVVTTMAFFIACVTSFSIFEKTSEEELQLKSFSISVRKYLPCFTFLSRIIQYLFLISVITMVLLTLMTVTLDPPQKLPDLFSVLVCFVSCLNFLFFLVYFNIIIMWDSKSGRNQKKIS
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Molecular Weight
58.1 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
ALG6 (Asparagine-linked glycosylation 6) is an essential protein involved in the process of N-glycosylation, which is critical for the proper folding, stability, and function of many proteins in eukaryotic cells. This enzyme is responsible for the transfer of a specific oligosaccharide precursor to nascent polypeptides in the endoplasmic reticulum (ER), a step that is vital for ensuring that proteins attain their correct conformation before proceeding to the Golgi apparatus for further modification. Mutations in the ALG6 gene have been linked to congenital disorders of glycosylation, which can result in severe developmental and neurological defects in affected individuals. The study of ALG6 and its recombinant protein form is crucial not only for understanding the molecular mechanisms underlying these diseases but also for exploring potential therapeutic strategies. Moreover, due to its pivotal role in glycosylation, ALG6 has garnered interest in biopharmaceutical production, as the proper glycosylation of therapeutic proteins is vital for their efficacy and safety. Research on ALG6 encompasses structural analyses to better understand its enzymatic function, the development of model systems for studying glycosylation defects, and the exploration of its potential as a target for drug design. Overall, the investigation of ALG6 recombinant protein continues to be a significant area of study with implications for both basic biology and clinical applications.
