Analytical Data
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Gene name
Sialidase-1
- Application
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Alternative Names
NEU1; SIAL1; Sialidase 1; Lysosomal Sialidase; Acetylneuraminyl hydrolase; G9 sialidase; N-acetyl-alpha-neuraminidase 1
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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
Q99519
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Expression Region
Met1~Gln380
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Molecular Weight
70kDa
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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
Sialidase-1, also known as neuraminidase-1 (NEU1), is an important enzyme that catalyzes the removal of sialic acid residues from glycoconjugates, playing a crucial role in cellular processes such as cell signaling, pathogen recognition, and immune responses. Mutations or deficiencies in the NEU1 gene are linked to sialidosis and other lysosomal storage disorders, which can lead to severe neurological symptoms, developmental delays, and other metabolic issues. Research on recombinant Sialidase-1 protein focuses on its biosynthesis, structural characterization, and functional analysis to understand its role in various biological processes and disease mechanisms. The production of recombinant NEU1 provides an opportunity for therapeutic applications, including enzyme replacement therapy, to alleviate symptoms associated with NEU1 deficiencies. Recent advancements in protein engineering and expression systems have facilitated the development of highly active and stable recombinant forms of the enzyme, paving the way for potential clinical interventions. Additionally, understanding the enzymatic mechanisms and substrate specificity of sialidase-1 may lead to innovative strategies for targeting diseases related to glycan metabolism and provide insights into the broader implications of sialylation in health and disease. Overall, ongoing research aims to harness the therapeutic potential of recombinant Sialidase-1 in treating sialidosis and other related conditions while advancing our understanding of the critical roles that sialic acid plays in cellular functions and pathogenicity.
