Analytical Data
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Gene name
MAGOH
- Application
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Alternative Names
Mago nashi homolog proliferation associated (Drosophila); Mago nashi protein homolog; magoh; MAGOHA; MGN_HUMAN; Protein mago nashi homolog
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61326
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Expression Region
1-146aa
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Molecular Weight
44.2 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
MAN1A2, a member of the mannosidase family, plays a crucial role in the glycosylation process, particularly in the maturation of N-linked glycoproteins within the endoplasmic reticulum. This enzyme catalyzes the hydrolysis of mannose residues in high-mannose oligosaccharides, contributing to the proper folding and functionality of glycoproteins. Research into MAN1A2 has gained significant attention due to its involvement in various physiological and pathological processes, including cell signaling, immune response, and disease mechanisms. Abnormalities in glycosylation linked to MAN1A2 deficiencies have been associated with several disorders, including congenital disorders of glycosylation (CDGs) and cancers. Moreover, understanding the structure and function of MAN1A2 could provide insights into therapeutic strategies for these diseases. The recombinant production of MAN1A2 has enabled detailed biochemical and structural studies, allowing researchers to elucidate its catalytic mechanisms and interactions with substrates and inhibitors. This line of research not only enhances our understanding of glycoprotein biosynthesis but also paves the way for potential applications in biotechnology and medicine, such as the development of glycoprotein-based therapeutics and diagnostic tools. Thus, MAN1A2 represents a significant focus in glycoscience, with implications for both fundamental research and practical applications in health and disease management.
