Abstract
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.
Highlights
2.2 Cloning ProcessGalectin-3 is widely expressed in adult tissues, on and secreted by activated macrophages, monocytes and adipocytes [1]
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
SDS-PAGE analysis demonstrated that recombinant galectin protein was efficiently and inducible expressed in inclusion body form and could dissolve in 6 M urea
Summary
2.2 Cloning ProcessGalectin-3 is widely expressed in adult tissues, on and secreted by activated macrophages, monocytes and adipocytes [1]. Galectin-3 dimers can crosslink cell surface glycoproteins of various cells, causing cell activation [2]. They can mediate cell-cell and cell-extracellular matrix adhesion by serving as a bridge to bind cells together or cells to extracellular matrix proteins [3]. Extracellular functions include the modulation of cell-substrate or cell-cell adhesion, cell migration, cell activation, proliferation and survival [4]. In this way, galectin is an important factor during the immune response, cancer progression, chronic inflammation and infection [5,6,7,8]. Conclusion: Characterization studies clearly revealed that the purified protein was galectin 3.
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