Analytical Data
-
Gene name
acylamidase
- Application
-
Alternative Names
Arylalkyl acylamidase; EC 3.5.1.76; Fragment
-
Species
Pseudomonas putida
-
Source
E. coli
-
Tag
Tag Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P35902
-
Expression Region
1-28aa
-
Molecular Weight
3.1 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
Acylamidase is an important enzyme that catalyzes the hydrolysis of N-acylamide compounds, crucial in various biochemical pathways and industrial applications. The increasing concerns over the toxicity of certain acylamide compounds, which are found in processed foods and certain industrial processes, have heightened the need for effective biocatalysts capable of detoxifying these substances. Research into the recombinant expression of acylamidase has gained traction as it opens avenues for producing large quantities of the enzyme with desirable properties, such as enhanced stability and activity under diverse conditions. The development of recombinant acylamidase not only helps in understanding the enzyme's structure-function relationship but also holds promise for environmental bioremediation and the food industry, as it can potentially be used to reduce the levels of harmful acylamides in food products. Furthermore, the study of recombinant acylamidase contributes to a broader understanding of enzyme evolution and the adaptability of microbial systems to metabolize various substrates, indicating its significance in both fundamental biochemistry and applied biotechnology.
