http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-103091498-B
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_42d90e70c0d612b8587fbe897976d33a |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-63 |
| filingDate | 2013-01-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate | 2014-12-31-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_98976598e0153ea4a01521cc63121987 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_8ebc37866ecdc015530b0404b031bb22 |
| publicationDate | 2014-12-31-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | CN-103091498-B |
| titleOfInvention | Plant in-vitro ubiquitin protein degradation system and application thereof |
| abstract | The invention discloses a plant in-vitro ubiquitin protein degradation system and an application thereof. The plant in-vitro ubiquitin protein degradation system provided by the invention is a composition consisting of one ubiquitin activating enzyme from arabidopsis thaliana, 14 ubiquitin-conjugating enzymes and wild-type K48R and K63R point mutation ubiquitin protein. Compared with the currently common used in-vitro ubiquitination reaction component, all components of the composition provided by the invention come from the model plant arabidopsis thaliana; when the composition is used for detecting whether the to-be-detected protein of plant origin has ubiquitination activity, the analysis result is more real and credible; the composition provided by the invention contains the component capable of representing most of the subfamily characteristics of the ubiquitin-conjugating enzyme of arabidopsis thaliana, and the coverage is wide; the activity of ubiquitin ligase can be detected and the specific binding condition of E2-E3 can be analyzed more comprehensively by use of the components, and more clues can be provided for studying the gene functions; and moreover, the type of polyubiquitin chain formed by the ubiquitination reaction can be analyzed by use of the point mutation ubiquitin protein. |
| priorityDate | 2013-01-08-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 111.