isopropyl-thiogalactoside and Carcinoma--Hepatocellular

isopropyl-thiogalactoside has been researched along with Carcinoma--Hepatocellular* in 2 studies

Other Studies

2 other study(ies) available for isopropyl-thiogalactoside and Carcinoma--Hepatocellular

ArticleYear
Production of a Novel Multi-Epitope Peptide Vaccine against Hepatocellular Carcinoma.
    Iranian journal of medical sciences, 2022, Volume: 47, Issue:6

    Hepatocellular carcinoma (HCC) is one of the prevalent cancers in the world with a high recurrence rate. In recent years, different researches have focused on designing efficient multi-epitope peptide vaccines against HCC. In designing these vaccines, over-expressed antigens in HCC patients, such as α- fetoprotein (AFP) and glypican-3 (GPC-3), have been employed. In our previous study, a multi-epitope peptide vaccine for HCC was designed by. This research is experimental and was carried out in Fasa, Iran, in 2017. The designed vaccine construct gene was transformed to the. The best conditions for protein expression were obtained in the Super Optimal Broth (SOB) medium at 37 °C after the induction of expression by 1 mM IPTG for six hour.. The recombinant HCC vaccine was produced with a proper concentration.

    Topics: alpha-Fetoproteins; Carcinoma, Hepatocellular; Epitopes; Humans; Isopropyl Thiogalactoside; Liver Neoplasms; Vaccines, Subunit

2022
Expression of human peroxisome proliferator-activated receptors ligand binding domain-maltose binding protein fusion protein in Escherichia coli: a convenient and reliable method for preparing receptor for screening ligands.
    Assay and drug development technologies, 2008, Volume: 6, Issue:6

    Human peroxisome proliferator-activated receptors (hPPARs) are ligand-activated transcription factors and are the target for the treatment of many diseases. Screening of their ligands is mainly based on assays of ligand binding to the ligand binding domain (LBD) of hPPARs.However, such assays are difficult because of the preparation of hPPARs LBD. In order to yield functional hPPARs LBD for screening ligands, hPPARs LBD was fused with maltose-binding protein(MBP) using the pMAL-p2x expression system through the gene engineering technique. The radioligand binding assay showed that MBP did not affect ligand binding with hPPARs LBD in the fusion proteins, which means that MBP-hPPARs LBD can be used instead of hPPARs LBD in ligand screening work. The results show that the new strategy using MBP as a fusion tag for preparing hPPARs LBD for screening ligands is a convenient and reliable method. It may be used to easily obtain the other nuclear receptors.

    Topics: Amylose; Arachidonic Acid; Binding Sites; Carcinoma, Hepatocellular; Carrier Proteins; Chromatography, Affinity; Chromatography, DEAE-Cellulose; DNA, Complementary; Drug Evaluation, Preclinical; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Factor Xa; Humans; Isopropyl Thiogalactoside; Ligands; Male; Maltose-Binding Proteins; Peroxisome Proliferator-Activated Receptors; Recombinant Fusion Proteins; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Transcription Factors

2008