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Title 

Expression of recombinant Lym-1 single-chain Fv in Escherichia coli

Authors 

Kyung Bin SongMi Sun WonClaude F Meares

Publisher 

Portland Press

Issue Date 

1998

Citation 

Biotechnology and Applied Biochemistry, vol. 28, no. 2, pp. 163-167

Keywords 

amino acid sequenceantibodies, monoclonalantigens, surfaceB-lymphocytesbase sequencechromatography, affinitycircular dichroismenzyme-linked immunosorbent assayescherichia coligene expression

Abstract 

Lym-1 single-chain Fv (sFv) can be used for targeted radiodiagnosis and therapy of B-lymphocytic malignancies. Lym-1 sFv was constructed and expressed as a glutathione S-transferase fusion protein, using a (G4S)3 linker connecting the C-terminus of the VH domain and the N-terminus of the VL domain of Lym-1. Six histidine residues and an E Tag epitope were introduced at the C-terminus of the sFv. Lym-1 sFv was purified with glutathione-Sepharose 4B affinity chromatography followed by digestion with thrombin. Lym-1 sFv of 28 kDa was confirmed by Western blotting with anti-(E Tag) monoclonal antibody. An antigen binding assay of Lym-1 and a CD study indicated that it is functionally active.

ISSN 

0885-4513

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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