Analytical Data
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Gene name
NCU05495
- Application
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Alternative Names
NCU05495Cyanovirin-N homolog; CV-N homolog
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Species
Neurospora crassa
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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
Q7S6U4
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Expression Region
1-111aa
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Molecular Weight
16.9 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
NCU05495 is a recombinant protein derived from *Neurospora crassa*, a model organism widely studied in fungal genetics and cell biology. This protein has garnered attention due to its potential role in various cellular processes, including metabolic regulation and stress response. Research into NCU05495 is significant as it may contribute to a better understanding of fungal biology, including growth, development, and adaptation mechanisms. The characterization of this protein can also yield insights into its functional properties, which may be crucial for applications in biotechnology and agriculture. Additionally, studying NCU05495 may help elucidate evolutionary aspects of fungal proteomes, drawing parallels with similar proteins in other organisms. The recombinant expression of this protein allows for the examination of its structure and activity in controlled conditions, facilitating detailed biochemical studies. As such, NCU05495 represents a valuable target for research aimed at unraveling the complexities of fungal physiology and exploring its applications in various fields, including enzyme development and biocontrol strategies in agriculture. Understanding the mechanisms underlying its function could open up new avenues for utilizing fungal proteins in industrial applications and improve crop resilience against environmental stresses. Overall, the investigation of NCU05495 is positioned at the intersection of fundamental research and practical applications, highlighting its potential significance in both scientific and agricultural contexts.
