Source:http://linkedlifedata.com/resource/pubmed/id/10868798
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2000-9-21
|
pubmed:abstractText |
Secretory phospholipase A2 (PLA2) consists of several 14-kDa isoforms with extensive homology, which makes it difficult to identify a specific isoform. In this study, we have developed and characterized monoclonal antibodies (MAbs) directed specifically against human group V sPLA2 (hVPLA2) derived from cultured hybridomas. These hybridomas were produced from the fusion of BALB/c-derived myeloma s/p20-Ag14 and splenocytes from mice immunized with purified recombinant hVPLA2. Three hybridomas secreting MAbs, MCL-3G1, MCL-2A5, and MCL-1B7, were selected and subcloned on the basis of their specificity to recognize hVPLA2 using solid-phase enzyme-linked immunoadsorbent assay (ELISA). The purified MAbs demonstrated a common pattern of immunoreactivity to hVPLA2, but not to human group IIa isoform (hIIaPLA2). Isotype analysis indicates that these hybridomas are of the IgG1 type. Under reducing conditions, MCL-3G1 sensitively detected hVPLA2 and demonstrated no cross-reactivity to either hIIaPLA2 or group IV cytosolic PLA2. Although specific for hVPLA2, a relatively modest signal was recognized with MCL-1B7 and MCL-2A5. These newly developed MAbs allow for determination of tissue distribution and cell-specific functions of hVPLA2.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Group V Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0272-457X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
19
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
171-6
|
pubmed:dateRevised |
2007-11-15
|
pubmed:meshHeading |
pubmed-meshheading:10868798-Animals,
pubmed-meshheading:10868798-Antibodies, Monoclonal,
pubmed-meshheading:10868798-Blotting, Western,
pubmed-meshheading:10868798-Cross Reactions,
pubmed-meshheading:10868798-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:10868798-Group V Phospholipases A2,
pubmed-meshheading:10868798-Humans,
pubmed-meshheading:10868798-Hybridomas,
pubmed-meshheading:10868798-Immunoglobulin G,
pubmed-meshheading:10868798-Mice,
pubmed-meshheading:10868798-Mice, Inbred BALB C,
pubmed-meshheading:10868798-Phospholipases A,
pubmed-meshheading:10868798-Phospholipases A2,
pubmed-meshheading:10868798-Protein Isoforms,
pubmed-meshheading:10868798-Recombinant Proteins
|
pubmed:year |
2000
|
pubmed:articleTitle |
Characterization of monoclonal antibodies specific for 14-kDa human group V secretory phospholipase A2 (hVPLA2).
|
pubmed:affiliation |
Department of Medicine, The University of Chicago, IL 60637, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|