Analytical Data
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Gene name
ALG13
- Application
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Alternative Names
ALG13; ALG13. S. cerevisiae. homolog of; ALG13. UDP-N-acetylglucosaminyltransferase subunit
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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
Q9NP73
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Expression Region
1-165aa
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AA Sequence
MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDVYRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTCSTLPGLLQSMDLSTLKCYPPGQPEKFSAFLDKVVGLQK
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Molecular Weight
44.6 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
Related Products
Protein Description
ALG13 (mannosyl-oligosaccharide 1,2-alpha-mannosidase) is a crucial enzyme involved in the biosynthesis of N-glycans, which are essential for proper protein folding and function. Mutations in the ALG13 gene can lead to a rare genetic disorder known as ALG13-related intellectual disability, characterized by developmental delays and neurological impairment. This highlights the importance of understanding the enzyme's structure and function. The research surrounding recombinant ALG13 protein focuses on elucidating its biochemical properties and the mechanism by which it catalyzes the transfer of mannose residues in oligosaccharide biosynthesis. By generating and characterizing recombinant ALG13, researchers aim to dissect its role in glycosylation pathways and how alterations in its activity can lead to disease. Additionally, studying ALG13 provides insights into potential therapeutic approaches for managing disorders linked to glycosylation defects. The development of recombinant sources of the enzyme also opens avenues for biotechnological applications, such as in the production of glycoproteins with desired properties for therapeutic use. Overall, the investigation of recombinant ALG13 protein serves as a fundamental step in understanding the broader implications of glycosylation in health and disease.
