Analytical Data
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Gene name
NEU2
- Application
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Alternative Names
Cytosolic sialidase (N-acetyl-alpha-neuraminidase 2)
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Species
Cricetulus griseus
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q64393
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Expression Region
1-379aa
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Molecular Weight
44.0
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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
NEU2, a member of the neuraminidase family of enzymes, has garnered significant attention in the field of biomedical research due to its role in the cleavage of sialic acid residues from glycoproteins and glycolipids. This enzymatic activity is crucial for various biological processes, including cell signaling, immune response, and cellular interactions. Abnormalities in sialylation patterns, which NEU2 might influence, have been implicated in several pathologies, including cancer progression and neurological disorders. The recombinant production of NEU2 protein has proved essential for elucidating its structural and functional properties, enabling researchers to investigate its mechanisms of action and potential therapeutic applications. Various expression systems have been employed to generate active NEU2, facilitating purification and characterization efforts. Understanding NEU2's enzymatic activity at the molecular level could provide insights into its substrate specificity and catalytic mechanisms, enhancing our knowledge of glycan biology. Furthermore, as the interest in targeting glycosylation processes for drug development rises, NEU2 presents promising avenues for therapeutic interventions and biomarker identification in disease contexts, underscoring the importance of continued research on this recombinant protein.
