Analytical Data
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Gene name
NEU
- Application
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Alternative Names
NEU；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
P04626
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Expression Region
720-976aa
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AA Sequence
LRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEF
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Molecular Weight
36.6 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
Related Products
Protein Description
The study of NEU (sialidase or neuraminidase) recombinant proteins is significant due to their crucial role in various biological processes and disease mechanisms. NEU enzymes, which cleave sialic acid residues from glycoproteins and glycolipids, are implicated in many physiological and pathological conditions, including viral infections, cancer progression, and autoimmune diseases. Understanding the structure and function of NEU proteins is essential for developing therapeutic interventions, as these enzymes can influence cell signaling, immune responses, and pathogen interactions. Recombinant technology allows for the production of NEU proteins in controlled environments, facilitating detailed studies of their enzymatic activity and potential applications in drug development. Moreover, the ability to manipulate NEU proteins through genetic engineering enhances the prospects for designing specific inhibitors or therapeutics that target these enzymes, offering new avenues for treatment strategies. The increasing recognition of the importance of sialylation in cellular processes further underscores the need for research into NEU recombinant proteins, aiming to elucidate their biological roles and harness their potential in biotechnology and medicine.
