Analytical Data
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Gene name
nrdB
- Application
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Alternative Names
nrdB；P53r2；Ribonucleoside-diphosphate reductase subunit M2 B
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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
P69924
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Expression Region
2-376aa
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AA Sequence
AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL
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Molecular Weight
45.4 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
NrdB is a crucial subunit of ribonucleotide reductase, an enzyme responsible for converting ribonucleotides into deoxyribonucleotides, which are essential for DNA synthesis and repair. In bacteria, the enzyme exists in two forms: the aerobic class I and the anaerobic class II, with NrdB typically associated with the class I family found in many Gram-negative and Gram-positive organisms. Research on NrdB and its recombinantly expressed protein has gained significance due to its potential implications in antimicrobial development, as inhibiting ribonucleotide reductase can hinder bacterial growth by depleting deoxynucleotides necessary for DNA replication. Moreover, NrdB serves as a model for studying enzyme mechanics, regulation, and protein-protein interactions within the ribonucleotide reductase complex. Advances in recombinant DNA technology have enabled the production of NrdB in expression systems, facilitating detailed biochemical studies and structural analysis. Investigations into the kinetics, substrate specificity, and structure-function relationships of NrdB can provide insights into its role in cellular metabolism and its potential as a target for drug design, particularly in combating resistant strains of bacteria. As antibiotic resistance becomes a growing global concern, understanding the molecular mechanisms governing NrdB could pave the way for novel therapeutic strategies, underscoring the relevance of recombinant NrdB protein research in the broader context of infectious disease management and biochemistry.
