Analytical Data
-
Gene name
Lysine decarboxylase
- Application
-
Alternative Names
Klebsiella pneumoniae IS43; Lyase
-
Species
Others
-
Source
E. coli
-
Tag
His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
W1DIY2
-
Expression Region
M1-K715
-
Protein Length
Partial
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Lysine decarboxylase (LDC) is an important enzyme that catalyzes the decarboxylation of lysine to produce cadaverine, a compound involved in various biological processes, including amino acid metabolism and cell signaling. The study of LDC has gained traction due to its potential applications in biotechnology and medicine, particularly in the synthesis of polyamines and as a target for antimicrobial drug development. In many organisms, LDC plays a crucial role in stress response mechanisms, enabling cells to adapt to unfavorable conditions by modulating intracellular pH and promoting cell growth. Recent advances in recombinant protein technology have facilitated the isolation and characterization of LDC from different sources, allowing researchers to explore its structural and functional properties in greater depth. By generating recombinant LDC, scientists can investigate the enzyme’s kinetics, substrate specificity, and regulatory mechanisms, providing insights into its role in metabolic networks. Moreover, the expression of LDC in heterologous systems offers strategies for enhancing its production, paving the way for industrial applications in various fields, including food preservation and bioproduction. Understanding the functional dynamics of LDC not only underscores its biological significance but also highlights its potential as a biotechnological tool for addressing contemporary challenges in health and industry. This growing body of research contributes to a broader understanding of amino acid metabolism and the development of innovative approaches for enzyme engineering and application. As the demand for sustainable and efficient bioprocesses increases, LDC research presents promising avenues for future exploration and innovation.











