Open AccessImproving the Recombinant Protein Expression of Human Galectin-3 in BL21 Bacterial Host System
Author(s) -
Praveen Kumar Vemuri,
Varakala Nikhil Reddy,
Divyanshu Dhakate,
Tripura Ravavarapu,
Faina Philberta Dumpala,
Susmita Sri Muddana,
Haritha Bommepalli,
Spurthi Modiboyana
Publication year - 2020
Publication title -
journal of pharmaceutical research international
Language(s) - English
Resource type - Journals
ISSN - 2456-9119
DOI - 10.9734/jpri/2020/v32i3430970
Subject(s) - glycobiology , recombinant dna , glycan , glycosylation , affinity chromatography , glycoprotein , escherichia coli , biochemistry , secretion , galectin , biology , chemistry , gene , enzyme
Background: Regardless of the broad explore in the territory of glycobiology concerning structure and capacity of glycans, lectins and glycosylation forms, numerous viewpoints are still left unexplored.
Aim: In this study, we analyzed the effect of shuttle vector on the secretion of human galectin recombinant protein.
Methods: The galectin was expressed in E. coli BL21 by growing the bacterial culture in SOC medium and purified by nickel-based affinity chromatography due to its His-tag.
Results: After cell lysis the protein was identified as a single 29 KDa band by 12% SDS-PAGE. Conclusion: Characterization studies clearly revealed that the purified protein was indeed galectin 3.