Analytical Data
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Gene name
panD
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简介
The panD protein plays a crucial role in cellular metabolism by catalyzing the pyruvyl-dependent decarboxylation of aspartate, thereby producing β-alanine. This enzyme activity represents a key step in the biosynthesis of pantothenic acid (vitamin B5), since beta-alanine is the precursor for the formation of this important cofactor. panD Protein, Corynebacterium jeikeium (FLAG, His) is the recombinant panD protein, expressed by E. coli , with N-6*His, N-Flag labeled tag.
- Application
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Alternative Names
panD; Aspartate 1-decarboxylase; Aspartate alpha-decarboxylase
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Species
Others
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Source
E. coli
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Tag
N-6*His;N-Flag
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q4JXL3
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Expression Region
M1-A138
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Protein Length
Full Length
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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
PanD is a pivotal protein that plays a critical role in the biosynthesis of coenzyme A (CoA) in various organisms, including bacteria and eukaryotes. It is involved in the conversion of pantothenate (vitamin B5) to 4'-phosphopantothenate, a key intermediate in the CoA synthesis pathway. Recent research has underscored the importance of PanD in microbial metabolism and its potential as a target for antimicrobial drug development, given that CoA is essential for numerous biochemical reactions including fatty acid synthesis, the Krebs cycle, and the metabolism of carbohydrates and amino acids. The study of PanD recombinant proteins has gained traction, allowing scientists to explore its structural characteristics and enzymatic functions in detail. By utilizing recombinant DNA technology, researchers can produce PanD proteins in heterologous systems, enabling sophisticated biochemical assays and crystallographic studies that reveal insights into its catalytic mechanisms and interactions with substrates and inhibitors. This knowledge may pave the way for innovative therapeutic strategies to combat bacterial infections, as inhibiting PanD activity could disrupt cellular metabolism crucial for bacterial growth and survival. Thus, the research on PanD recombinant proteins not only enhances our understanding of fundamental biological processes but also holds promise for the development of novel antimicrobial agents targeting the CoA biosynthesis pathway.
