Analytical Data
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Gene name
ALG1
- Application
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Alternative Names
beta-1.4-mannosyltransferase homolog (S. cerevisiae); Asparagine-linked glycosylation Protein 1 homolog; Beta 1 4 mannosyltransferase; Beta-1
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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
Q9BT22
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Expression Region
1-464aa
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AA Sequence
MAASCLVLLALCLLLPLLLLGGWKRWRRGRAARHVVAVVLGDVGRSPRMQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLGSMHSPFRARSEPEDPVTERSAFTERDAGSGLVTRLRERPALLVSSTSWTEDEDFSILLAALEKFEQLTLDGHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQLQMLFSNFPDPAGKLNQFRKNLRESQQLRWDESWVQTVLPLVMDT
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Molecular Weight
52.5 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
ALG1, or asparagine-linked glycosylation 1, is a critical enzyme involved in the glycosylation process, specifically in the assembly of the pre-assembled high-mannose oligosaccharides that are essential for proper protein folding and stability in the endoplasmic reticulum. Research on ALG1 has gained attention due to its pivotal role in protein maturation, and its dysfunction is linked to various congenital disorders of glycosylation (CDGs), which can lead to severe developmental and neurological anomalies. The manipulation and study of ALG1 recombinant proteins have become crucial in understanding the molecular mechanisms underlying these diseases, as well as the broader implications of glycosylation in cellular processes. By exploring the structure-function relationships of ALG1 and its interactions with other glycosylation machinery, researchers aim to elucidate the pathway's intricacies, potentially leading to therapeutic interventions for CDGs and related disorders. Additionally, the production of recombinant ALG1 proteins facilitates high-throughput screenings for potential inhibitors or enhancers of its enzymatic activity, thereby providing valuable insights into drug development. The advancements in biotechnology have allowed for the effective expression and purification of ALG1, making it a model system for glycosylation studies. Through comprehensive studies of ALG1 and its role in glycan biosynthesis, scientists are striving to unravel the complexities of glycosylation, which remains an essential aspect of understanding protein biochemistry and its implications in health and disease management.
