Pharmacological characterization of new β-agonists using Huβ1- and Huβ2-adrenergic receptor binding assay in transfected HEK-293 cells

2005 ◽  
Vol 529 (1-2) ◽  
pp. 53-56 ◽  
Author(s):  
Cinzia Civitareale ◽  
Caterina Ambrosio ◽  
Maria Sbraccia ◽  
Maurizio Fiori ◽  
Gianfranco Brambilla ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Adrenergic Receptor ◽  
Binding Assay ◽  
Pharmacological Characterization ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
Receptor Binding Assay ◽  
293 Cells

scholarly journals Biophysical and Pharmacological Characterization of Nav1.9 Voltage Dependent Sodium Channels Stably Expressed in HEK-293 Cells

PLoS ONE ◽  
2016 ◽  
Vol 11 (8) ◽  
pp. e0161450 ◽  
Author(s):  
Zhixin Lin ◽  
Sonia Santos ◽  
Karen Padilla ◽  
David Printzenhoff ◽  
Neil A. Castle
Keyword(s):  
Sodium Channels ◽  
Pharmacological Characterization ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
293 Cells ◽  
Voltage Dependent

scholarly journals Pharmacological characterization of small-conductance Ca2+ -activated K+ channels stably expressed in HEK 293 cells

2000 ◽  
Vol 129 (5) ◽  
pp. 991-999 ◽  
Author(s):  
Dorte Strøbaek ◽  
Tino D Jørgensen ◽  
Palle Christophersen ◽  
Philip K Ahring ◽  
Søren-Peter Olesen
Keyword(s):  
Pharmacological Characterization ◽  
Hek 293 ◽  
K Channels ◽  
Hek 293 Cells ◽  
293 Cells ◽  
Small Conductance

Functional Characterization of the Regulatory Region of Human CD2-Associated Protein Promoter in HEK 293 Cells

2009 ◽  
Vol 29 (3) ◽  
pp. 203-212 ◽  
Author(s):  
Xin-Ming Su ◽  
Wei Ren ◽  
Chao Lu ◽  
Ji-Qing Chen ◽  
Sheng-Hua Wu ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Regulatory Region ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
293 Cells

Characterization of glycine release mediated by glycine transporter 1 stably expressed in HEK-293 cells

1997 ◽  
Vol 49 (1-2) ◽  
pp. 89-94 ◽  
Author(s):  
Kazuko Sakata ◽  
Kohji Sato ◽  
Patrick Schloss ◽  
Heinrich Betz ◽  
Shoichi Shimada ◽  
...  
Keyword(s):  
Hek 293 ◽  
Hek 293 Cells ◽  
Glycine Release ◽  
Glycine Transporter 1 ◽  
Glycine Transporter ◽  
293 Cells

scholarly journals Characterization of a human 5-hydroxytryptamine3 receptor type A (h5-HT3R-AS) subunit stably expressed in HEK 293 cells

1996 ◽  
Vol 118 (5) ◽  
pp. 1237-1245 ◽  
Author(s):  
Anthony G. Hope ◽  
John A. Peters ◽  
Angus M. Brown ◽  
Jeremy J. Lambert ◽  
Thomas P. Blackburn
Keyword(s):  
Type A ◽  
Receptor Type ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
293 Cells

scholarly journals Characterization of bovine interleukin-2 stably expressed in HEK-293 cells

2020 ◽  
Author(s):  
Shuya MITOMA ◽  
Heba M. EL-KHAIAT ◽  
Tomofumi UTO ◽  
Katsuaki SATO ◽  
Satoshi SEKIGUCHI ◽  
...  
Keyword(s):  
Interleukin 2 ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
293 Cells

scholarly journals The nuts and bolts of SARS-CoV-2 Spike Receptor Binding Domain heterologous expression

2021 ◽  
Author(s):  
Mariano Maffei ◽  
Linda C Montemiglio ◽  
Grazia Vitagliano ◽  
Luigi Fedele ◽  
Shaila Sellathurai ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Neutralizing Antibodies ◽  
Gel Filtration ◽  
Binding Domain ◽  
Model Systems ◽  
Receptor Binding Domain ◽  
Binding Ability ◽  
Hek 293 ◽  
293 Cells

COVID-19 is a highly infectious disease caused by a newly emerged coronavirus (SARS-CoV-2) that has rapidly progressed into a pandemic. This unprecedent emergency has stressed the significance of developing effective therapeutics to fight current and future outbreaks. The receptor-binding domain (RBD) of the SARS-CoV-2 surface Spike protein is the main target for vaccines and represents a helpful tool to produce neutralizing antibodies or diagnostic kits. In this work, we provide a detailed characterization of the native RBD produced in three major model systems: Escherichia coli, insect and HEK-293 cells. Circular dichroism, gel filtration chromatography and thermal denaturation experiments indicated that recombinant SARS-CoV-2 RBD proteins are stable and correctly folded. In addition, their functionality and receptor-binding ability were further evaluated through ELISA, flow cytometry assays and bio-layer interferometry.

scholarly journals Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion

2003 ◽  
Vol 370 (1) ◽  
pp. 19-28 ◽  
Author(s):  
Slavoljub VUJCIC ◽  
Ping LIANG ◽  
Paula DIEGELMAN ◽  
Debora L. KRAMER ◽  
Carl W. PORTER
Keyword(s):  
Northern Blot Analysis ◽  
Biochemical Characterization ◽  
Polyamine Oxidase ◽  
Preference Ranking ◽  
Hek 293 ◽  
Hek 293 Cells ◽  
Polyamine Analogues ◽  
293 Cells ◽  
Back Conversion

In the polyamine back-conversion pathway, spermine and spermidine are first acetylated by spermidine/spermine N1-acetyltransferase (SSAT) and then oxidized by polyamine oxidase (PAO) to produce spermidine and putrescine respectively. Although PAO was first purified more than two decades ago, the protein has not yet been linked to genomic sequences. In the present study, we apply a BLAST search strategy to identify novel oxidase sequences located on human chromosome 10 and mouse chromosome 7. Homologous mammalian cDNAs derived from human brain and mouse mammary tumour were deduced to encode proteins of approx. 55kDa having 82% sequence identity. When either cDNA was transiently transfected into HEK-293 cells, intracellular spermine pools decreased by approx. 30%, whereas spermidine increased 2—4-fold. Lysates of human PAO cDNA-transfected HEK-293 cells, but not vector-transfected cells, rapidly oxidized N1-acetylspermine to spermidine. Substrate specificity determinations with the lysate assay revealed a preference ranking of N1-acetylspermine = N1-acetylspermidine>N1,N12-diacetylspermine>spermine; spermidine was not acted upon. This ranking is identical to that reported for purified PAO and distinctly different from the recently identified spermine oxidase (SMO), which prefers spermine over N1-acetylspermine. Monoethyl- and diethylspermine analogues also served as substrates for PAO, and were internally cleaved adjacent to a secondary amine. We deduce that the present oxidase sequences are those of the FAD-dependent PAO involved in the polyamine back-conversion pathway. In Northern blot analysis, PAO mRNA was much less abundant in HEK-293 cells than SMO or SSAT mRNA, and all three were differentially induced in a similar manner by selected polyamine analogues. The identification of PAO sequences, together with the recently identified SMO sequences, provides new opportunities for understanding the dynamics of polyamine homoeostasis and for interpreting metabolic and cellular responses to clinically-relevant polyamine analogues and inhibitors.

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