Analytical Data
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Gene name
dapA
- Application
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Alternative Names
dapA；4-hydroxy-tetrahydrodipicolinate synthase
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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
P0A6L2
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Expression Region
1-292aa
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AA Sequence
MFTGSIVAIVTPMDEKGNVCRASLKKLIDYHVASGTSAIVSVGTTGESATLNHDEHADVVMMTLDLADGRIPVIAGTGANATAEAISLTQRFNDSGIVGCLTVTPYYNRPSQEGLYQHFKAIAEHTDLPQILYNVPSRTGCDLLPETVGRLAKVKNIIGIKEATGNLTRVNQIKELVSDDFVLLSGDDASALDFMQLGGHGVISVTANVAARDMAQMCKLAAEGHFAEARVINQRLMPLHNKLFVEPNPIPVKWACKELGLVATDTLRLPMTPITDSGRETVRAALKHAGLL
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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
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Protein Description
DapA, or diaminopimelate aminotransferase, is an essential enzyme in the lysine biosynthesis pathway of many bacteria, making it a critical target for antibiotic development. The enzyme catalyzes the conversion of L-aspartate 4-semialdehyde to meso-diaminopimelate, an intermediate vital for peptidoglycan biosynthesis in bacterial cell walls. Given its absence in mammals, DapA presents a promising target for the development of new antimicrobial agents that can selectively inhibit bacterial growth without affecting human cells. Research on recombinant DapA proteins has gained momentum in recent years, as characterizing these proteins can shed light on their structure-function relationships and provide insights into potential inhibitors. Various methods, including cloning, expression in heterologous systems, and biochemical assays, have been employed to investigate DapA’s enzymatic activity and stability. Additionally, understanding the regulatory mechanisms that modulate DapA activity can contribute to the development of novel therapeutic strategies against antibiotic-resistant bacterial strains. This research not only furthers our understanding of bacterial metabolism but also holds potential for the advancement of next-generation antibiotics.
