Analytical Data
-
Gene name
ldcA
- Application
-
Alternative Names
LD-carboxypeptidase AMuramoyltetrapeptide carboxypeptidase
-
Species
Escherichia coli
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P76008
-
Expression Region
1-304aa
-
Molecular Weight
37.6 kDa
-
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
LdcA (Lysine Decarboxylase A) is an enzyme widely studied for its role in lysine metabolism and its implications in various biological processes. Found in several bacterial species, LdcA catalyzes the decarboxylation of lysine to produce cadaverine, a compound linked to stress response and growth regulation. Research on LdcA has gained momentum due to its potential applications in biotechnology, including biofuel production, bioremediation, and the development of probiotic strains. Moreover, understanding the enzyme's structure and function can provide insights into microbial ecology and the mechanisms of antibiotic resistance, as certain bacteria utilize LdcA to survive in hostile environments. Genetic manipulation and recombinant protein expression have enabled scientists to produce LdcA in heterologous systems, facilitating detailed kinetic studies and structure-function analyses. The study of LdcA not only augments our understanding of microbial physiology but also opens avenues for engineering metabolic pathways in industrial applications. Consequently, the exploration of LdcA and its recombinant forms continues to be an important focus in microbiology and biochemistry, emphasizing its significance in both fundamental research and applied sciences.
