Analytical Data
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Gene name
MAN1A1
- Application
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Alternative Names
HUMM3; HUMM9; MAN9; Mannosyl-Oligosaccharide 1,2-Alpha-Mannosidase IA; Mannosidase alpha class 1A member 1; Processing alpha-1,2-mannosidase IA
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P33908
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Expression Region
Ile322~Glu653
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Molecular Weight
68kDa
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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
MAN1A1 (Mannosidase Alpha Class 1A Member 1) is an important enzyme involved in the process of N-glycosylation, a critical post-translational modification that affects protein folding, stability, and function. The enzyme catalyzes the hydrolysis of specific mannose residues in the sugar chains attached to proteins, playing a pivotal role in the maturation of glycoproteins within the endoplasmic reticulum. Aberrations in MAN1A1 activity have been linked to various diseases, including cancer, neurodegenerative disorders, and congenital disorders of glycosylation, highlighting its relevance in health and disease. Given the significance of glycosylation in biological systems, the study of MAN1A1 recombinant protein has gained momentum, aiming to elucidate its structural and functional characteristics, as well as its enzymatic mechanisms. The expression and purification of recombinant MAN1A1 allow researchers to investigate its role in glycoprotein biosynthesis and to explore potential therapeutic applications. Additionally, understanding the enzyme's regulatory dynamics can provide insights into the larger network of glycosylation processes and their implications in cellular physiology. Thus, research on MAN1A1 not only enhances our comprehension of fundamental biological processes but also holds promise for the development of targeted interventions for related diseases.
