Linked Life Data

15350852

Source:http://linkedlifedata.com/resource/pubmed/id/15350852

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-9-7
pubmed:abstractText
Phospholamban (PLB) and calsequestrin (CSQ) play important roles in sarcoplasmic reticulum Ca(2+) transport and storage in cardiac muscle. Specific antibodies have been frequently used to quantitate CSQ and PLB protein levels. Here we demonstrate that two of the commonly available anti-PLB antibodies, anti-PLB-2D12 and anti-PLB-A1, show lower reactivity to phosphorylated than dephosphorylated PLB. A custom anti-PLB antibody, generated using a peptide corresponding to amino acids 2-14, is not affected by the phosphorylation state of PLB. In contrast, anti-CSQ reacts less with dephosphorylated CSQ than with phosphorylated CSQ. All three commercially available antibodies tested in this study have been widely used to quantify PLB and CSQ expression, and the results are integrated in many publications. Our studies reveal that the phosphorylation status of PLB and CSQ can affect antibody reactivity and may lead to over- or underestimation of the relative protein content and erroneous interpretation of data.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2828
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
795-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Phosphorylation-status of phospholamban and calsequestrin modifies their affinity towards commonly used antibodies.
pubmed:affiliation
Department of Physiology and Cell Biology, The Ohio State University College of Medicine and Public Health, 304 Hamilton Hall, 1645 Neil Avenue, Columbus, OH 43210, USA.
pubmed:publicationType
Journal Article