Analytical Data
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Gene name
NEU2
- Application
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Alternative Names
NEU2；ARVP；VP；Vasopressin-neurophysin 2-copeptin
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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
Q9Y3R4
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Expression Region
180-268aa
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AA Sequence
AYRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQ RVVTLNARSHLRARVQAQSTNDGLDFQESQLVKKLVEPP
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Molecular Weight
35 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
NEU2 is a sialidase, an enzyme that hydrolyzes sialic acid residues from glycoconjugates, playing a crucial role in various biological processes, including cell signaling, immune response, and pathogen recognition. Research on NEU2 has gained momentum due to its potential implications in cancer progression, neurodegenerative diseases, and viral infections, where altered sialylation patterns can affect cellular interactions and functionalities. Moreover, sialidases like NEU2 may contribute to the modulation of the tumor microenvironment and enhance the migratory capabilities of cancer cells, making them a target for therapeutic intervention. The recombinant expression of NEU2 allows for in-depth studies of its enzymatic activity, substrate specificity, and regulatory mechanisms. Recent advancements in protein engineering and expression systems have facilitated the production of active NEU2, permitting investigations into its structure-function relationships and interactions with other biomolecules. Understanding NEU2’s role in both physiological and pathological contexts is essential for developing novel strategies for disease treatment and prevention, emphasizing the importance of continued research in dissecting the functional properties of this enzyme.
