pubmed-article:17948000 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17948000 | lifeskim:mentions | umls-concept:C1257988 | lld:lifeskim |
pubmed-article:17948000 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
pubmed-article:17948000 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:17948000 | pubmed:dateCreated | 2007-10-19 | lld:pubmed |
pubmed-article:17948000 | pubmed:abstractText | Protein phosphorylation plays important roles in various aspects of cellular events. Visualization of site-specific phosphorylation in cells is of great importance not only to analyze spatial and temporal distribution but also to investigate biological function. Now, site- and phosphorylation state-specific antibodies are widely utilized as the most powerful tools for these analyses. This protocol details a method to produce the polyclonal version of such an antibody by immunizing a synthetic phosphopeptide corresponding to a protein phosphorylated at targeted site(s). This protocol is also applicable to the production of other types of antibodies, which specifically recognize the site-specific modification, such as acetylation, methylation and proteolysis. The protocol can be completed in 2-3 months. | lld:pubmed |
pubmed-article:17948000 | pubmed:language | eng | lld:pubmed |
pubmed-article:17948000 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17948000 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17948000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17948000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17948000 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17948000 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17948000 | pubmed:issn | 1750-2799 | lld:pubmed |
pubmed-article:17948000 | pubmed:author | pubmed-author:InagakiMasaki... | lld:pubmed |
pubmed-article:17948000 | pubmed:author | pubmed-author:GotoHidemasaH | lld:pubmed |
pubmed-article:17948000 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17948000 | pubmed:volume | 2 | lld:pubmed |
pubmed-article:17948000 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17948000 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17948000 | pubmed:pagination | 2574-81 | lld:pubmed |
pubmed-article:17948000 | pubmed:dateRevised | 2008-3-24 | lld:pubmed |
pubmed-article:17948000 | pubmed:meshHeading | pubmed-meshheading:17948000... | lld:pubmed |
pubmed-article:17948000 | pubmed:meshHeading | pubmed-meshheading:17948000... | lld:pubmed |
pubmed-article:17948000 | pubmed:meshHeading | pubmed-meshheading:17948000... | lld:pubmed |
pubmed-article:17948000 | pubmed:meshHeading | pubmed-meshheading:17948000... | lld:pubmed |
pubmed-article:17948000 | pubmed:meshHeading | pubmed-meshheading:17948000... | lld:pubmed |
pubmed-article:17948000 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17948000 | pubmed:articleTitle | Production of a site- and phosphorylation state-specific antibody. | lld:pubmed |
pubmed-article:17948000 | pubmed:affiliation | Division of Biochemistry, Aichi Cancer Center Research Institute, Nagoya, Aichi 464-8681, Japan. | lld:pubmed |
pubmed-article:17948000 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17948000 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17948000 | lld:pubmed |