Analytical Data
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Gene name
NRPS1
- Application
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Alternative Names
NRPS1；pes1；pesB；Nonribosomal peptide synthetase 1
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Species
E.coli
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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
Q4WT66
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Expression Region
894-1342aa
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AA Sequence
LSPIQKLHFMVRKEGQGYFNQSVVTRIDRQINDQDMRRAVEAVVMRHSMLRSRLVDPSTGNSLQLRITEDVAGSYRWRTHYMTAQNEIENAIAESQLCINAFVGPVFAVDFCYVDEDSHNLLSLVAHHLVVDIVSWRIILEDLEDFLLNPQGFVLQNSSLPFQTWCRLQDEQCESVAFENDVQLEDLPAPDLAYWGMEHRQMTYGDVICETFELDPGSTQSILLECHQSLRTEPVDLFLAALVHSFGQTFPERTLPVIYNEGHGREVWDSSLDISRTVGWFTTLYPIFVQEIVSEDPARTVARVKDLRRQVSDNGRQKFASRMFTGKGQQTCRHHYPLEMTFNYVGQHRDLQKQDGLFQLMGHMAGEAGQGGGAADFGEETPRFALLEISALVVQGQLRFTFSFNRFMRHQSGIHAWISRCHQLLASLGQKLQSLAPQPTLSDFPMLSL
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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 (Non-Ribosomal Peptide Synthetase 1) is a multifunctional enzyme that plays a critical role in the biosynthesis of non-ribosomal peptides, which are essential for various biological functions and possess significant pharmaceutical potential. These peptides, unlike ribosomal peptides, are synthesized through a modular assembly line mechanism, enabling the production of a diverse range of compounds with intricate structures. The study of NRPS1 has gained prominence due to its involvement in the production of bioactive metabolites, including antibiotics, immunosuppressants, and anticancer agents. Researchers are particularly interested in understanding the structure and function of NRPS1 to harness its capabilities for biotechnological applications. The exploration of its enzymatic activity, substrate specificity, and the regulatory mechanisms governing its expression can provide valuable insights for synthetic biology, allowing for the engineered production of novel compounds with therapeutic relevance. Moreover, understanding NRPS1 activity can lead to advancements in drug discovery, particularly in the context of emerging antibiotic resistance, where novel antimicrobial peptides could offer new avenues for treatment.
