Steven Gutteridge - Wilmington DE, US Timothy Caspar - Yorklyn DE, US Daniel Cordova - Hockessin DE, US James J. Rauh - Conowingo MD, US Rejane M. Smith - Elkton MD, US Lihong Wu - Newark DE, US Yong Tao - Newark DE, US
Assignee:
E. I. du Pont de Nemours and Company - Wilmington DE
International Classification:
C07K 14/00 A61K 38/16
US Classification:
530350, 514 12
Abstract:
The genes encoding ryanodine receptor homologs have been characterized from multiple insect families including lepidopteran tobacco budworm (), homopteran green peach aphid (), corn plant hopper (), cotton melon aphid () and fruitfly (). The full-length genes have been isolated, cloned and amplified in bacterial cells. Expression in insect cells shows that the recombinant protein folds into a functional calcium release channel. The genes and their corresponding polypeptides have a number of uses including, but not limited to, the isolation of other pest ryanodine receptors, the development of screens to identify insecticidally active compounds, use of fragments of genes as pesticides, fragments of protein for antibody production, fragments of protein for determination of the structure of insecticide binding sites, and identification of insecticides that disrupt the calcium balance in cells through other messengers that interact with the receptor calcium release mechanism. Methods are outlined for overcoming toxic effects of expressing recombinant proteins in host cells.
Timothy Casper - Yorklyn DE, US Daniel Cordova - Hockessin DE, US Steven Gutteridge - Wilmington DE, US James J Rauh - Conowingo MD, US Rejane M Smith - Elkton MD, US Lihong Wu - Newark DE, US Yong Tao - Newark DE, US
Assignee:
E.I. du Pont de Nemours and Company - Wilmington DE
International Classification:
C12Q 1/00 C12Q 1/68 G01N 33/53
US Classification:
435 4, 435 6, 435 71
Abstract:
The genes encoding ryanodine receptor homologs have been characterized from multiple insect families including lepidopteran tobacco budworm (), homopteran green peach aphid (), corn plant hopper (), cotton melon aphid () and fruitfly (). The full-length genes have been isolated, cloned and amplified in bacterial cells. Expression in insect cells shows that the recombinant protein folds into a functional calcium release channel. The genes and their corresponding polypeptides have a number of uses including, but not limited to, the isolation of other pest ryanodine receptors, the development of screens to identify insecticidally active compounds, use of fragments of genes as pesticides, fragments of protein for antibody production, fragments of protein for determination of the structure of insecticide binding sites, and identification of insecticides that disrupt the calcium balance in cells through other messengers that interact with the receptor calcium release mechanism. Methods are outlined for overcoming toxic effects of expressing recombinant proteins in host cells.
Steven Gutteridge - Wilmington DE, US Timothy Caspar - Yorklyn DE, US Daniel Cordova - Hockessin DE, US James Rauh - Conowingo MD, US Yong Tao - Newark DE, US Lihong Wu - Newark DE, US Rejane Smith - Elkton MD, US
The genes encoding ryanodine receptor homologs have been characterized from multiple insect families including lepidopteran tobacco budworm (), homopteran green peach aphid (), corn plant hopper (), cotton melon aphid () and fruitfly (). The full-length genes have been isolated, cloned and amplified in bacterial cells. Expression in insect cells shows that the recombinant protein folds into a functional calcium release channel. The genes and their corresponding polypeptides have a number of uses including, but not limited to, the isolation of other pest ryanodine receptors, the development of screens to identify insecticidally active compounds, use of fragments of genes as pesticides, fragments of protein for antibody production, fragments of protein for determination of the structure of insecticide binding sites, and identification of insecticides that disrupt the calcium balance in cells through other messengers that interact with the receptor calcium release mechanism. Methods are outlined for overcoming toxic effects of expressing recombinant proteins in host cells.
Steven Gutteridge - Wilmington DE, US Timothy Caspar - Yorklyn DE, US Daniel Cordova - Hockessin DE, US James J. Rauh - Conowingo MD, US Yong Tao - Newark DE, US Lihong Wu - Newark DE, US Rejane M. Smith - Elkton MD, US
Assignee:
E. I. DU PONT DE NEMOURS AND COMPANY - Wilmington DE
The genes encoding ryanodine receptor homologs have been characterized from multiple insect families including lepidopteran tobacco budworm (), homopteran green peach aphid (), corn plant hopper (), cotton melon aphid () and fruitfly (). The full-length genes have been isolated, cloned and amplified in bacterial cells. Expression in insect cells shows that the recombinant protein folds into a functional calcium release channel. The genes and their corresponding polypeptides have a number of uses including, but not limited to, the isolation of other pest ryanodine receptors, the development of screens to identify insecticidally active compounds, use of fragments of genes as pesticides, fragments of protein for antibody production, fragments of protein for determination of the structure of insecticide binding sites, and identification of insecticides that disrupt the calcium balance in cells through other messengers that interact with the receptor calcium release mechanism. Methods are outlined for overcoming toxic effects of expressing recombinant proteins in host cells.
Steven Gutteridge - Wilmington DE, US Timothy Caspar - Yorklyn DE, US Daniel Cordova - Hockessin DE, US James J. Rauh - Conowingo MD, US Yong Tao - Newark DE, US Lihong Wu - Newark DE, US Rejane M. Smith - Elkton MD, US
Assignee:
E.I. DU PONT DE NEMOURS AND COMPANY - Wilmington DE
The genes encoding ryanodine receptor homologs have been characterized from multiple insect families. The genes and their corresponding polypeptides have a number of uses including but not limited to the development of screens to identify insecticidally active compounds. Methods are outlined for overcoming toxic effects of expressing recombinant proteins in host cells.
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