Analytical Data
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Gene name
ALG2
- Application
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Alternative Names
AIP1; ALG 2; ALG-2-interacting Protein 1; ALG2; ALIX; Apoptosis linked gene 2
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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
O75340
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Expression Region
1-416aa
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AA Sequence
MAEEQGRERDSVPKPSVLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFAESRELPVRCAGDWLPRGLGWGGRGAAVCAYVRMVFLALYVLFLADEEFDVVVCDQVSACIPVFRLARRRKKILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVFKETFKSLSHIDPDVLYPSLNVTSFDSVVPEKLDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLTSQDWERVHLIVAGGYDERVLENVEHYQELKKMVQQSDLGQYVTFLRSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEPDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQLYRYVTKLLV
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Molecular Weight
73.5 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
ALG2, or Alpha-1,3-mannosyltransferase, is a crucial protein involved in the glycosylation process within the endoplasmic reticulum, specifically in the biosynthesis of N-glycans. It plays a significant role in protein folding and quality control, influencing various biological processes and cellular functions. Research into ALG2 and its recombinant protein has gained momentum due to its links to multiple diseases, including certain cancers and genetic disorders related to protein misfolding, such as congenital disorders of glycosylation (CDGs). The production of recombinant ALG2 allows researchers to study its structure-function relationships, explore its enzymatic mechanisms, and evaluate its potential as a therapeutic target. Moreover, understanding ALG2's role in cellular signaling pathways and its interactions with other glycosyltransferases can enhance our comprehension of glycosylation's impact on human health. As scientists unlock the complexities of ALG2 and its glycosylation patterns, they may uncover new insights into disease mechanisms, paving the way for innovative treatments. This emerging field of study holds promise for advancing personalized medicine and developing strategies to correct glycosylation defects, ultimately improving patient outcomes in related disorders. Thus, ALG2 recombinant protein research is vital for unraveling the intricate interplay between glycosylation and human diseases.
