Publications (2)1.59 Total impact
-
Article: An efficient expression and purification strategy for the production of S100 proteins in Escherichia coli.
[show abstract] [hide abstract]
ABSTRACT: S100 proteins belong to a family of small, acidic, EF-hand Ca ( 2+) -binding proteins and have been found to exert both intracellular and extracellular functions in regulation of Ca ( 2+) homeostasis, cytoskeletal dynamics, cell cycle, motility and differentiation. As a result, they have been widely investigated for their association with diseases, such as, neurological diseases, cardiomyopathy, neoplasias and inflammatory diseases. To facilitate further studies of S100 proteins, we reported a simple and efficient method for the expression and purification of human S100A4 and S100A11 proteins in Escherichia coli. Since S100 proteins share many common physical and chemical characteristics, we expect that this approach can be extended to the production of most S100 proteins.Bioengineered. 09/2012; 4(1). -
Article: Expression and purification of bioactive high-purity human S100A6 in Escherichia coli.
[show abstract] [hide abstract]
ABSTRACT: S100A6, as a member of S100 protein family, have biological functions in cell proliferation, differentiation, morphology, cytoskeletal organization and apoptosis. In the last three decades, S100A6 has been caught more and more attention. Here, we introduced a simple and efficient method for producing high-purity recombinant human S100A6 from Escherichia coli culture with low level of endotoxin. We further demonstrated its biological activities for triggering SH-SY5Y cells apoptosis in vitro. These results can facilitate the study of physiological and pathological roles of S100A6 and other members of S100 family proteins.Protein Expression and Purification 03/2012; 83(1):98-103. · 1.59 Impact Factor
Top co-authors
Top Journals
Institutions
-
2012
-
Shanghai Jiao Tong University
- School of Agriculture and Biology
Shanghai, Shanghai Shi, China
-
