Data on optimization of expression and purification of AIMP2-DX2 protein in Escherichia coli

نویسندگان

  • Roshan Jha
  • Hye Young Cho
  • Ameeq Ul Mushtaq
  • Kiho Lee
  • Dae Gyu Kim
  • Sunghoon Kim
  • Young Ho Jeon
چکیده

AIMP2-DX2 is a splicing variant of AIMP2 protein which has been implicated in human lung cancer and chemoresistance of ovarian cancer (J.W. Choi, D.G. Kim, A.E. Lee, H.R. Kim, J.Y. Lee, N.H. Kwon, et al., 2011; J.W. Choi, J.W. Lee, J.K. Kim, H.K. Jeon, J.J. Choi, D.G. Kim, et al., 2012) [1,2]. We have shown, here, the data for the expression of AIMP2-DX2 protein in Escherichia coli and optimization of the critical steps in purification of AIMP2-DX2. The data described here has been successfully used to get a maximum yield of highly pure AIMP2-DX2 for subsequent characterization of its biophysical property in: "Purification and biophysical characterization of the AIMP2-DX2 protein" (R. Jha, H.Y. Cho, A. Ul Mushtaq, K. Lee, D.G. Kim, S. Kim, et al., 2017) [3].

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Cloning and evaluation of gene expression and purification of gene encoding recombinant protein containing binding subunit of coli surface antigens CS1 and CS2 from Enterotoxigenic Escherichia coli

Background & Objective: Enterotoxigenic Escherichia coli (ETEC) is a major causative agent of diarrhea. Enterotoxins and the colonization factors (CFs) are major virulence factors in ETEC infections. The bacterium binds to the intestinal epithelial cell surface through colonization factors and produces enterotoxins that cause excessive fluid and electrolyte secretion in the lumen of the intesti...

متن کامل

Optimization of secretory expression of recombinant hGM-CSF in high cell density cultivation of recombinant Escherichia coli using Taguchi statistical method

Human granulocyte macrophage colony stimulating factor (hGM-CSF) has many therapeutic applications.In this study, in order to verify the purification process, the effect of carbon source, IPTG concentration andpost-induction time on the secretion of recombinant hGM-CSF into the culture medium by recombinantEscherichia coli during high cell density cultivation were evaluated by...

متن کامل

Enhanced Expression of Recombinant Activin A in Escherichia coli by Optimization of Induction Parameters

Activin A is a member of the transforming growth factor β super family. Because of its extensive clinical usages, its recombinant production is beneficial. In this study, activin A was expressed in E. coli using the pET 21a expression vector. The optimization of the activin A production in E. coli was done by using the response surface methodology (RSM). At this stage, the effect of IPTG and la...

متن کامل

Optimization of Cloning Conditions for high-level Production of Recombinant Mouse Interleukin-2 in Escherichia coli

Backgrounds and objectives: Interleukin 2 (IL-2) secreted by activated CD4+ T cells  has been known as a major mediator in both  adaptive and native immune system  due to a board range of effects on  different cells in the immunity system (1-6). Methods: cDNA synthesis was performed using gene- specific primers designed by Gene Runner software after RNA extraction of mouse splenocytes. PCR pro...

متن کامل

Ratio of Autoantibodies of Tumor Suppressor AIMP2 and Its Oncogenic Variant Is Associated with Clinical Outcome in Lung Cancer

Aminoacyl-tRNA synthetase-interacting multi-functional protein 2 (AIMP2) works as potent tumor suppressor, while its splicing variant lacking exon 2 (AIMP2-DX2) competes with AIMP2 for binding to target proteins and compromises its anti-tumor activity. Assuming that AIMP2 and its variant AIMP2-DX2 could be released out to human sera in pathological condition, we investigated the diagnostic and ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره 11  شماره 

صفحات  -

تاریخ انتشار 2017