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|Title:||The Cys-rich and EGF-like domains of Carcinoscorpius rotundicauda Factor C yields soluble fusion protein with GFP||Authors:||Dwarakanath, R.S.
|Issue Date:||1997||Citation:||Dwarakanath, R.S.,Ho, B.,Ding, J.L. (1997). The Cys-rich and EGF-like domains of Carcinoscorpius rotundicauda Factor C yields soluble fusion protein with GFP. Biotechnology Letters 19 (11) : 1147-1150. ScholarBank@NUS Repository. https://doi.org/10.1023/A:1018461131484||Abstract:||The expression of the different domains of a complex serine protease, recombinant Factor C of the horseshoe crab, Carcinoscorpius rotundicauda, was achieved using pClneo and pEGFP-N1 vectors. In an in vitro coupled transcription-translation assay, the truncated CrFC cDNA insert coding for the initial 331 amino acids expressed the expected 36 kDa polypeptide lacking the antigenic epitopes. The highly disulfide-bonded Cys-rich and EGF-like domains at the N-terminus of CrFC which bind LPS were fused to GFP. When expressed in COS-1 cells, this fusion protein did not alter the localisation of the chromophore and remained soluble, indicating that other domains could be responsible for the membrane-bound nature of the recombinant Factor C, rFC. The expression of this LPS-binding domain of rFC as a soluble protein suggests possibilities of obtaining active rFC in mammalian cells.||Source Title:||Biotechnology Letters||URI:||http://scholarbank.nus.edu.sg/handle/10635/101890||ISSN:||01415492||DOI:||10.1023/A:1018461131484|
|Appears in Collections:||Staff Publications|
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