Analytical Data
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Gene name
dapA
- Application
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Alternative Names
dapA; b2478; JW2463; 4-hydroxy-tetrahydrodipicolinate synthase; HTPA synthase; EC 4.3.3.7
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Species
Escherichia coli
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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
P0A6L2
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Expression Region
1-292aa
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Molecular Weight
35.3 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 study of dapA, which encodes diaminopimelate aminotransferase, has garnered significant attention due to its critical role in bacterial lysine biosynthesis and the peptidoglycan layer formation. This enzyme catalyzes the conversion of L-aspartate-β-semialdehyde to meso-diaminopimelate, an essential intermediate in the lysine biosynthetic pathway, making it a potential target for antibiotic development. Researchers have focused on recombinant dapA protein to better understand its enzyme kinetics, structural characteristics, and catalytic mechanisms. Moreover, given the rising concern over antibiotic resistance, dapA provides a promising avenue for the development of new antimicrobial agents, particularly against Gram-negative pathogens, which often exhibit multidrug resistance. By engineering and characterizing dapA through recombinant DNA technology, scientists aim to elucidate its function, explore its potential as a drug target, and contribute to the design of novel therapeutic strategies. These efforts are integral to addressing public health challenges posed by resistant bacterial strains and enhancing our understanding of basic microbial metabolism. Through structural and functional analyses of the recombinant dapA protein, insights can be gained into its catalytic properties and interactions with inhibitors, paving the way for innovative approaches in antibiotic design aimed at disrupting bacterial growth and survival.
