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10.1074/mcp.O115.049957 http://scihub22266oqcxt.onion/10.1074/mcp.O115.049957 C4638049!4638049!26342038     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell+Proteomics 2015 ; 14 (11): 3094-104 Nephropedia Template TP {{tp|p=26342038|t=2015. Multiple Reaction Monitoring Enables Precise Quantification of 97 Proteins in Dried Blood Spots* |pdf=|usr=}}{{26342038}} gab.com Text Multiple Reaction Monitoring Enables Precise Quantification of 97 Proteins in Dried Blood Spots* JO: Mol Cell Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=26342038 #FOAvip The dried blood spot (DBS) methodology provides a minimally invasive approach to sample collection and enables room-temperature storage for most analytes. DBS samples have successfully been analyzed by liquid chromatography multiple reaction monitoring mass spectrometry (LC/MRM-MS) to quantify a large range of small molecule biomarkers and drugs; however, this strategy has only recently been explored for MS-based proteomics applications. Here we report the development of a highly multiplexed MRM assay to quantify endogenous proteins in human DBS samples. This assay uses matching stable isotope-labeled standard peptides for precise, relative quantification, and standard curves to characterize the analytical performance. A total of 169 peptides, corresponding to 97 proteins, were quantified in the final assay with an average linear dynamic range of 207-fold and an average R2 value of 0.987. The total range of this assay spanned almost 5 orders of magnitude from serum albumin (P02768) at 18.0 mg/ml down to cholinesterase (P06276) at 190 ng/ml. The average intra-assay and inter-assay precision for 6 biological samples ranged from 6.1?7.5% CV and 9.5?11.0% CV, respectively. The majority of peptide targets were stable after 154 days at storage temperatures from ?20 °C to 37 °C. Furthermore, protein concentration ratios between matching DBS and whole blood samples were largely constant (<20% CV) across six biological samples. This assay represents the highest multiplexing yet achieved for targeted protein quantification in DBS samples and is suitable for biomedical research applications. Twit Text FOAVip Multiple Reaction Monitoring Enables Precise Quantification of 97 Proteins in Dried Blood Spots* ????Mol Cell Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=26342038 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26342038 #FOAvip English Wikipedia <ref>{{Cite pmid|26342038}}</ref> Multiple Reaction Monitoring Enables Precise Quantification of 97 Proteins in Dried Blood Spots* #MMPMID26342038 Chambers AG; Percy AJ; Yang J; Borchers CH Mol Cell Proteomics 2015[Nov]; 14 (11): 3094-104 PMID26342038show ga The dried blood spot (DBS) methodology provides a minimally invasive approach to sample collection and enables room-temperature storage for most analytes. DBS samples have successfully been analyzed by liquid chromatography multiple reaction monitoring mass spectrometry (LC/MRM-MS) to quantify a large range of small molecule biomarkers and drugs; however, this strategy has only recently been explored for MS-based proteomics applications. Here we report the development of a highly multiplexed MRM assay to quantify endogenous proteins in human DBS samples. This assay uses matching stable isotope-labeled standard peptides for precise, relative quantification, and standard curves to characterize the analytical performance. A total of 169 peptides, corresponding to 97 proteins, were quantified in the final assay with an average linear dynamic range of 207-fold and an average R2 value of 0.987. The total range of this assay spanned almost 5 orders of magnitude from serum albumin (P02768) at 18.0 mg/ml down to cholinesterase (P06276) at 190 ng/ml. The average intra-assay and inter-assay precision for 6 biological samples ranged from 6.1?7.5% CV and 9.5?11.0% CV, respectively. The majority of peptide targets were stable after 154 days at storage temperatures from ?20 °C to 37 °C. Furthermore, protein concentration ratios between matching DBS and whole blood samples were largely constant (<20% CV) across six biological samples. This assay represents the highest multiplexing yet achieved for targeted protein quantification in DBS samples and is suitable for biomedical research applications. äMultiple Reaction Monitoring Enables Precise Quantification of 97 Prot(epmc).pdf DeepDyve Pubget Overpricing