Please use this identifier to cite or link to this item:
|Title:||The expression of soluble, full-length, recombinant human TSH receptor in a prokaryotic system.||Austin Authors:||Busuttil, Bridget E;Turney, K L;Frauman, Albert G||Affiliation:||Clinical Pharmacology and Therapeutics Unit, Department of Medicine, Austin and Repatriation Medical Centre, The University of Melbourne, Austin Campus, Heidelberg, Victoria, 3084, Australia||Issue Date:||1-Dec-2001||Publication information:||Protein Expression and Purification; 23(3): 369-73||Abstract:||For the first time soluble, full-length, recombinant, human thyroid-stimulating hormone (TSH) receptor (TSHR) has been expressed in a prokaryotic system. The full-length TSHR cDNA, obtained from normal human thyroid, was cloned into a pQE-9 vector, sequenced, and confirmed to be identical to the published sequence, to be full length, and to be in frame. Expression of the receptor was as a fusion protein with a hexahistidine tail at the amino terminal, in an Escherichia coli expression system. Approximately 2.5 mg of protein per liter of bacterial culture was recovered from the cell homogenate, after a single passage through a nickel-nitrilotriacetic acid resin column. An estimated 60% increase in purity of a band of expected size, 87 kDa, was observed upon gel electrophoresis and staining with Coomassie blue, after the single purification step. Immunoreactivity of the 87-kDa protein with Graves' sera was confirmed by Western blotting.||Gov't Doc #:||11722172||URI:||http://ahro.austin.org.au/austinjspui/handle/1/9360||DOI:||10.1006/prep.2001.1519||URL:||https://pubmed.ncbi.nlm.nih.gov/11722172||Type:||Journal Article||Subjects:||Amino Acid Sequence
Receptors, Thyrotropin.genetics.immunology.isolation & purification.metabolism
Recombinant Fusion Proteins.isolation & purification.metabolism
|Appears in Collections:||Journal articles|
Show full item record
checked on Nov 30, 2022
Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.