Analytical Data
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Gene name
NRPS1
- Application
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Alternative Names
NRPS1; pes1; pesB; AFUA_1G10380; Nonribosomal peptide synthetase 1; EC 6.3.2.-
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Species
eosartorya fumigata
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q4WT66
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Expression Region
894-1342aa
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Molecular Weight
67.2 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
NRPS1, or Non-Ribosomal Peptide Synthetase 1, is a crucial enzyme involved in the biosynthesis of non-ribosomal peptides, which are structurally diverse and often exhibit significant pharmacological activities. These peptides play critical roles in various biological processes and are known for their potential as therapeutic agents, including antibiotics, anticancer compounds, and immunosuppressants. The study of NRPS1 is particularly important because it provides insights into the mechanisms behind peptide synthesis that do not rely on ribosomes, contrasting with the traditional protein production pathway. This enzyme operates through a modular architecture, allowing for the incorporation of various building blocks, thus increasing the diversity of the resulting peptides. Understanding the structure and function of NRPS1 can lead to advancements in drug discovery and development, as synthetic biology techniques can be employed to engineer NRPS pathways for the production of novel compounds. The exploration of NRPS1 also has implications in biotechnology and synthetic chemistry, expanding the potential for producing valuable bioactive substances. Consequently, ongoing research aims to elucidate the intricate mechanisms of NRPS1, optimize its function, and explore its applications in producing new pharmaceuticals, making it a significant focus in the fields of microbiology, biochemistry, and drug development.
