Analytical Data
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Gene name
aprN
- Application
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Alternative Names
Nattokinase
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Species
Bacillus subtilis subsp. natto
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Source
E. coli
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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
P35835
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Expression Region
107-381aa
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Molecular Weight
31.8 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 aprN gene, which encodes for the enzyme AprN, plays a crucial role in various biological processes, particularly concerning bacterial pathogenicity and biofilm formation. This gene is known for its involvement in the synthesis of extracellular polysaccharides, which are vital for bacterial adherence and virulence. The study of aprN recombinant proteins has gained significant attention in recent years due to their potential applications in developing novel therapeutic strategies against infectious diseases. By producing and characterizing these recombinant proteins, researchers aim to understand their structural and functional properties, which can elucidate the mechanisms underlying bacterial virulence. The implications of aprN studies extend beyond microbial pathogenesis, as they can contribute to vaccine development, diagnostics, and the design of inhibitors that target polysaccharide biosynthesis pathways. As antibiotic resistance continues to challenge current treatment options, exploring the role of aprN and its recombinant products offers promising avenues for innovative interventions in medical microbiology. Overall, the investigation of aprN recombinant proteins represents a vital area of research that bridges fundamental microbiological principles with practical applications in combating bacterial infections.
