Analytical Data
-
Gene name
entD
- Application
-
Alternative Names
entD；ENTH domain-containing Protein 1
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P20723
-
Expression Region
26-258aa
-
AA Sequence
NENIDSVKEKELHKKSELSSTALNNMKHSYADKNPIIGENKSTGDQFLENTLLYKKFFTDLINFEDLLINFNSKEMAQHFKSKNVDVYPIRYSINCYGGEIDRTACTYGGVTPHEGNKLKERKKIPINLWINGVQKEVSLDKVQTDKKNVTVQELDAQARRYLQKDLKLYNNDTLGGKIQRGKIEFDSSDGSKVSYDLFDVKGDFPEKQLRIYSDNKTLSTEHLHIDIYLYEK
-
Molecular Weight
42.9 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
EntD is a member of the non-ribosomal peptide synthetase (NRPS) superfamily and plays a crucial role in the biosynthesis of entamycin, a potent antibiotic produced by certain strains of Streptomyces. This enzyme is involved in the modification of substrate molecules and facilitates the assembly of various peptide units into complex structures. The study of entD and its recombinant protein has garnered interest due to its potential applications in developing novel antibiotics as the global threat of antibiotic resistance continues to rise. Researchers have sought to understand the enzymatic mechanisms and structural characteristics of EntD to exploit its capabilities for engineering new bioactive compounds. Advances in recombinant DNA technology have enabled the expression of entD in heterologous systems, allowing for detailed functional analyses and the potential modification of the resulting peptides. This research could pave the way for innovative therapeutic strategies by furnishing insights into natural product biosynthesis and facilitating the design of synthetic analogs with enhanced activity or reduced toxicity. As part of the larger effort to combat microbial resistance and discover new antibiotics, the exploration of entD and its protein products hold significant promise in microbial biotechnology and pharmaceutical development.
