Analytical Data
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Gene name
Neu4
- Application
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Alternative Names
Neu4；Sialidase-4
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Species
Mouse
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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
Q8BZL1
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Expression Region
1-478aa
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AA Sequence
MGPTRVPRRTVLFQRERTGLTYRVPALLCVPPRPTLLAFAEQRLSPDDSHAHRLVLRRGTLTRGSVRWGTLSVLETAVLEEHRSMNPCPVLDEHSGTIFLFFIAVLGHTPEAVQIATGKNAARLCCVTSCDAGLTWGSVRDLTEEAIGAALQDWATFAVGPGHGVQLRSGRLLVPAYTYHVDRRECFGKICWTSPHSLAFYSDDHGISWHCGGLVPNLRSGECQLAAVDGDFLYCNARSPLGNRVQALSADEGTSFLPGELVPTLAETARGCQGSIVGFLAPPSIEPQDDRWTGSPRNTPHSPCFNLRVQESSGEGARGLLERWMPRLPLCYPQSRSPENHGLEPGSDGDKTSWTPECPMSSDSMLQSPTWLLYSHPAGRRARLHMGIYLSRSPLDPHSWTEPWVIYEGPSGYSDLAFLGPMPGASLVFACLFESGTRTSYEDISFCLFSLADVLENVPTGLEMLSLRDKAQGHCWPS
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Molecular Weight
52.4 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
Neu4 is a sialidase enzyme that plays a crucial role in the metabolism of sialic acids, which are important components of glycoproteins and glycolipids on cellular surfaces. Research on Neu4 has garnered attention due to its potential implications in various biological processes, including cell signaling, immune response, and pathogen interaction. Dysregulation of sialidase activity has been associated with numerous health conditions, including cancer and neurodegenerative diseases. Understanding the structure, function, and regulatory mechanisms of Neu4 can provide insights into its role in physiology and pathology. Recent studies have focused on the enzyme's substrate specificity, catalytic mechanisms, and its potential as a therapeutic target. By using recombinant protein techniques, researchers can produce and characterize Neu4, paving the way for further investigations into its biological functions and clinical applications. The exploration of Neu4 could lead to novel strategies for cancer therapy and the development of specific inhibitors that modulate sialic acid metabolism, highlighting its significance in both basic research and clinical settings.
