Analytical Data
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Gene name
ALG5
- Application
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Alternative Names
ALG5; HSPC149Dolichyl-phosphate beta-glucosyltransferase; DolP-glucosyltransferase
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y673
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Expression Region
1-324aa
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AA Sequence
MAPLLLQLAVLGAALAAAALVLISIVAFTTATKMPALHRHEEEKFFLNAKGQKETLPSIWDSPTKQLSVVVPSYNEEKRLPVMMDEALSYLEKRQKRDPAFTYEVIVVDDGSKDQTSKVAFKYCQKYGSDKVRVITLVKNRGKGGAIRMGIFSSRGEKILMADADGATKFPDVEKLEKGLNDLQPWPNQMAIACGSRAHLEKESIAQRSYFRTLLMYGFHFLVWFLCVKGIRDTQCGFKLFTREAASRTFSSLHVERWAFDVELLYIAQFFKIPIAEIAVNWTEIEGSKLVPFWSWLQMGKDLLFIRLRYLTGAWRLEQTRKMN
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Molecular Weight
61.38 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
ALG5 (asparagine-linked glycosylation 5) is an essential enzyme involved in the process of N-glycosylation, a critical post-translational modification that influences protein folding, stability, and activity. The ALG5 gene encodes a UDP-GlcNAc:glycoprotein glucosyltransferase responsible for adding glucose residues to nascent glycoproteins in the endoplasmic reticulum. Proper functioning of ALG5 is crucial for the synthesis of correctly folded glycoproteins, which play key roles in cell signaling, immune response, and cellular transport. Mutations or dysfunctions in ALG5 have been implicated in various diseases, including congenital disorders and certain cancers, where aberrant glycosylation can lead to protein misfolding and aggregation. Research into ALG5 recombinant proteins aims to elucidate its structure-function relationships, investigate its enzymatic mechanisms, and explore potential therapeutic interventions. Recent studies have focused on the development of ALG5 inhibitors as prospective drug candidates, given the enzyme's significance in disease pathology. By producing and characterizing recombinant ALG5, researchers are not only advancing our understanding of glycosylation pathways but also paving the way for innovative treatments targeting glycosylation-related disorders.
