Journal: Clinical chemistry

Article Title: Ultrasensitive flow-based immunoassays using single-molecule counting.

doi: 10.1373/clinchem.2007.091181

Figure Lengend Snippet: Fig. 2. Goodness of curve fit; back interpolation of cTnI calibration curves generated over 8 consecutive assay runs [full range (A) and low end range (B) of quantification].

Article Snippet: Rat, dog, and monkey human cardiac troponin I (cTnI) were purified from natural sources and obtained from Hytest.

Techniques: Generated

Journal: Clinical chemistry

Article Title: Ultrasensitive flow-based immunoassays using single-molecule counting.

doi: 10.1373/clinchem.2007.091181

Figure Lengend Snippet: Fig. 3. Frequency distribution of cTnI in lithium heparin plasma specimens obtained from 100 blood donors.

Article Snippet: Rat, dog, and monkey human cardiac troponin I (cTnI) were purified from natural sources and obtained from Hytest.

Techniques: Clinical Proteomics

Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

Article Title: Protein Changes Contributing to Right Ventricular Cardiomyocyte Diastolic Dysfunction in Pulmonary Arterial Hypertension

doi: 10.1161/JAHA.113.000716

Figure Lengend Snippet: Sarcomeric protein phosphorylation. A, cTnI total phosphorylation was determined by ProQ‐Diamond staining, while total protein content was determined by SYPRO‐Ruby staining (n Don =10, n PAH =10). B, MyBPC total phosphorylation was determined by ProQ staining, while total protein content was determined by SYPRO staining (n Don =10, n PAH =10). C, Typical example of donor and PAH samples ProQ and SYPRO staining and the relative location of specific sarcomeric protein. ProQ staining annotations—ov, ovalbumin; β, β‐casein; MyBPC, myosin binding protein C; cTnT, cardiac troponin T; cTnI, cardiac troponin I; MLC 2 , myosin light chain 2. SYPRO staining annotations—MHC, myosin heavy chain. Data presented as mean±SEM. PAH inidcates pulmonary arterial hypertension.

Article Snippet: Blots were incubated with the following primary antibodies against specific protein or protein phosphorylation sites: cTnI dephosphorylated form (4T46, mouse monoclonal antibody, HyTest), cTnI PKA‐specific serine 22/23 site phosphorylation (4004, rabbit polyclonal antibody; Cell Signaling Technology).

Techniques: Phospho-proteomics, Staining, Binding Assay

Journal: Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease

Article Title: Protein Changes Contributing to Right Ventricular Cardiomyocyte Diastolic Dysfunction in Pulmonary Arterial Hypertension

doi: 10.1161/JAHA.113.000716

Figure Lengend Snippet: cTnI phosphorylation. A, Typical example of donor and PAH samples immunostained against the unphosphorylated form of cTnI and normalized for Ponceau‐S stained actin. cTnI total phosphorylation was determined by Western blot analysis in donor and PAH samples (n Don =8, n PAH =9). B, Typical example of donor and PAH samples immunostained against cTnI serine 22/23 residue and normalized for Ponceau‐S stained actin. cTnI serine 22/23 phosphorylation was determined by Western blot analysis in donor and PAH samples (n Don =9, n PAH =11). C, Typical example of donor and PAH samples immunostained against unphosphorylated (P 0 ) cTnI, mono‐phosphorylated (P 1 ) cTnI and bis‐phosphorylated (P 2 ) cTnI. cTnI relative phosphorylation distribution was determined by Phos‐Tag analysis in donor and PAH samples (n Don =5, n PAH =9). Data presented as mean±SEM. cTnI indicates cardiac troponin I; cTnT, cardiac troponin T; PAH, pulmonary arterial hypertension.

Article Snippet: Blots were incubated with the following primary antibodies against specific protein or protein phosphorylation sites: cTnI dephosphorylated form (4T46, mouse monoclonal antibody, HyTest), cTnI PKA‐specific serine 22/23 site phosphorylation (4004, rabbit polyclonal antibody; Cell Signaling Technology).

Techniques: Phospho-proteomics, Staining, Western Blot, Residue