Analytical Data
-
基因名
entD
- Application
-
别名
entD；ENTH domain-containing Protein 1
-
种属
E.coli
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P20723
-
表达区间
26-258aa
-
氨基酸序列
NENIDSVKEKELHKKSELSSTALNNMKHSYADKNPIIGENKSTGDQFLENTLLYKKFFTDLINFEDLLINFNSKEMAQHFKSKNVDVYPIRYSINCYGGEIDRTACTYGGVTPHEGNKLKERKKIPINLWINGVQKEVSLDKVQTDKKNVTVQELDAQARRYLQKDLKLYNNDTLGGKIQRGKIEFDSSDGSKVSYDLFDVKGDFPEKQLRIYSDNKTLSTEHLHIDIYLYEK
-
分子量
42.9 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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.
