Analytical Data
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Gene name
tdcD
- Application
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Alternative Names
tdcD；oxd-2；Propionate kinase
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Species
Human
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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
P59244
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Expression Region
1-402aa
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AA Sequence
MNEFPVVLVINCGSSSIKFSVLNASDCEVLMSGIADGINSENAFLSVNGGEPAPLAHHSYEGALKAIAFELEKRNLNDNVALIGHRIAHGGSIFTESAIITDEVIDNIRRVSPLAPLHNYANLSGIESAQQLFPGVTQVAVFDTSFHQTMAPEAYLYGLPWKYYEELGVRRYGFHGTSHRYVSQRAHSLLNLAEDDSGLVVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMSWVASQTNQSLGDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERAQLAIKTFVHRIARHIAGHAASLHRLDGIIFTGGIGENSSLIRRLVMEHLAVLGVEIDTEMNNRSNSFGERIVSSENARVICAVIPTNEEKMIALDAIHLGKVNAPAEFA
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Molecular Weight
50.4 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
TdcD, a key enzyme involved in the catabolism of tyrosine and phenylalanine, plays a crucial role in microbial metabolism, particularly in bacteria that utilize these amino acids as carbon and nitrogen sources. The protein is part of the tyrosine decarboxylase family, catalyzing the decarboxylation of tyrosine to produce tyramine, an important intermediate in various biochemical pathways. Research on TdcD has garnered interest due to its potential applications in biotechnology and medicine, particularly in the development of biocatalysts for the synthesis of pharmaceutical compounds and bioplastics. Additionally, understanding the structure and function of TdcD can shed light on the evolutionary adaptations of microbes in diverse environments. Recombinant expression and purification of TdcD enable detailed biochemical characterization and structural studies, which can provide insights into its catalytic mechanisms and regulatory processes. The functional analysis of TdcD, alongside comparative studies with related enzymes, contributes to a better understanding of microbial metabolism and its ecological significance, paving the way for innovative applications in metabolic engineering and synthetic biology. As researchers continue to explore the potential of TdcD, its diverse roles in microbial systems underscore the importance of functional enzymes in biotechnological advancements and ecological research.
