Troponin 1

Manufactured by Abcam

Sourced in United Kingdom, United States

Troponin I is a protein found in cardiac and skeletal muscle cells. It plays a crucial role in the regulation of muscle contraction by inhibiting the interaction between actin and myosin.

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Lab products found in correlation

Desmin, by GeneTex (2 mentions) Zen 2, by Zeiss (2 mentions) Axio imager m2 microscope, by Zeiss (2 mentions) Alexa fluor 647, by Jackson ImmunoResearch (2 mentions) β catenin, by Abcam (2 mentions) Ripa buffer, by Thermo Fisher Scientific (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Vector Laboratories (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (2 mentions) Wheat germ agglutinin (wga), by Thermo Fisher Scientific (2 mentions) Interleukin 6 (il 6), by Thermo Fisher Scientific (2 mentions) Il 1β, by Thermo Fisher Scientific (2 mentions) α smooth muscle actin, by Merck Group (1 mentions) Troponin t, by Abcam (1 mentions) Protease and phosphatase inhibitors, by Sangon (1 mentions) Stathmin, by Abcam (1 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) C jun, by Abcam (1 mentions) Flag tag (flag), by Beyotime (1 mentions) Enhanced chemi luminescence (ecl), by Merck Group (1 mentions) Vimentin, by Abcam (1 mentions)

Close spelling variants of this product

Anti-cardiac troponin I Rat Cardiac Troponin I SimpleStep ELISA Kit Troponin-I antibody Rabbit anti-troponin I antibody Cardiac troponin I (cTnI) Mouse troponin I Anti‐Troponin I Cardiac troponin I Human cardiac troponin I Rabbit anti-cardiac troponin I

12 protocols using troponin 1

Evaluating Myocardial Infarction Sequelae

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Mouse hearts 7 days post-MI were dehydrated in 30% sucrose solution, embedded in Tissue-Tek OCT compound, snap-frozen in dry ice, and then cut into 7 μm sections. The sections were then stained with a In Situ Cell Death Detection Kit (Roche Applied Science, CH), CD3, CD68, Troponin I (Abcam, United Kingdom), and DAPI (Vector Laboratories, Burlingame, CA, United States).
Mouse hearts 28 days post-MI were fixed in 10% formalin-PBS, then paraffin embedded, and cut into 3 μm sections. After deparaffinization, rehydration and tissue antigen recovery, the sections were stained with Periostin (R&D, United States), Troponin I (Abcam, United Kingdom), and DAPI (Vector Laboratories, Burlingame, CA, United States).

Zhao J., Chen Y., Chen Q., Hong T., Zhong Z., He J, & Ni C. (2022). Curcumin Ameliorates Cardiac Fibrosis by Regulating Macrophage-Fibroblast Crosstalk via IL18-P-SMAD2/3 Signaling Pathway Inhibition. Frontiers in Pharmacology, 12, 784041.

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Immunohistochemical Visualization of Human iCMs and iECs

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Immunohistochemical staining was carried out using the DAKO Animal Research Kit perioxidase system (Agilent), according to the manufacturer's instructions (Huang et al., 2005 (link)). Following deparaffinization, the tissue sections were treated with low pH antigen retrieval solution (Thermo Fisher) for epitope recovery at 100°C for 20 min. Immunofluorescence staining was performed as described above to visualize host murine endothelial cells and smooth muscle cells based on CD31 (BD Transduction Labs) and smooth muscle α-actin (SMA, Sigma), respectively. The contractile proteins troponin-T and troponin-I (both from Abcam), were used to visualize human iCMs, and a human-specific CD31 antibody (Dako) was used to visualize human iECs. Human and mouse tissues were used as positive and negative controls, respectively, to confirm species specificity.

Wanjare M., Kawamura M., Hu C., Alcazar C., Wang H., Woo Y.J, & Huang N.F. (2019). Vascularization of Engineered Spatially Patterned Myocardial Tissue Derived From Human Pluripotent Stem Cells in vivo. Frontiers in Bioengineering and Biotechnology, 7, 208.

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Western Blot Analysis of Cardiac Proteins

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Mechanically homogenised frozen hearts and fresh cell suspensions were lysed in RIPA buffer (Beyotime, China) with protease and phosphatase inhibitors (Sangon Biotech) on ice for 30 min. Protein concentrations were estimated using BCA assay (Beyotime) and subsequently adjusted to equal levels. Samples (30 μg) were loaded onto polyacrylamide gels and hybridised onto polyvinylidene difluoride membranes (Millipore, USA). Membranes were blocked with 5% BSA for 1 h and probed with the relevant primary antibodies for 16 h at 4°C. After washing, the membranes were incubated at room temperature for 1 h with appropriate secondary antibodies (CST, USA). The blots were developed using ECL (Millipore). The primary antibodies were GAPDH (CST, 5174), Cypher (Abnova, H00011155-M06), β-catenin (Abcam, 32572), β-catenin Ser675 (CST, 4176), β-catenin Ser552 (CST, 9566), β-catenin Ser33/37/Thr41 (CST, 9561), Gsk-3β (CST, 12456), Gsk-3β Ser9 (CST, 5558), vimentin (Abcam, 92547), vimentin Ser72 (Abcam, 52944), stathmin (Abcam, 52630), stathmin Ser16 (Abcam, 47382), troponin I (Abcam, 209809), troponin I Ser23+24 (Abcam, 190697), cyclin D1 (Abcam, 134175), c-Myc (Abcam, 32072), c-jun (Abcam, 32137), Myc (CST, 2276), Flag (Beyotime, AF519), and rabbit IgG (CST, 2729). The ImageJ software was used to quantify the relative protein levels.

Lv J., Pan Z., Chen J., Xu R., Wang D., Huang J., Dong Y., Jiang J., Yin X., Cheng H, & Guo X. (2021). Phosphoproteomic Analysis Reveals Downstream PKA Effectors of AKAP Cypher/ZASP in the Pathogenesis of Dilated Cardiomyopathy. Frontiers in Cardiovascular Medicine, 8, 753072.

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Cardiac Tissue Protein Analysis

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Cardiac tissue or cardiomyocyte lysates were prepared using ice-cold RIPA buffer (Thermo Fisher Scientific) containing Complete Protease Inhibitor Cocktail and PhosSTOP (Roche). Lysates or culture medium were cleared by centrifugation, reduced, subjected to Western blot using a NuPage system (Invitrogen), and probed with antibodies against TGF-β 1/2/3 (Santa Cruz Biotechnology), TGF-β (Abcam), Troponin I (Abcam), Smad6 (ab13727, Abcam), phospho-Smad1/5 (Thermo Fisher), and phospho-Smad2/3 (sc-11769, Santa Cruz Biotechnology).

Flevaris P., Khan S.S., Eren M., Schuldt A.J., Shah S.J., Lee D.C., Gupta S., Shapiro A.D., Burridge P.W., Ghosh A.K, & Vaughan D.E. (2017). Plasminogen Activator Inhibitor Type I Controls Cardiomyocyte Transforming Growth Factor-β and Cardiac Fibrosis. Circulation, 136(7), 664-679.

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Cardiac Aging Protein Expression

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Mice were euthanized by cervical dislocation and hearts from young and old animals were rapidly collected in cold PBS (1×) at 2 and 12 months. Macroscopic examination of the internal surface of the ventricles was performed as previously described [23 (link)]. Whole-mount and histological immunofluorescence and image analysis were carried out as previously described [19 (link)]. Antibodies used in this study are specific to Nkx2-5 (Sc8697 Santa-Cruz, Dallas, TX, USA), GFP (AbD Serotec, Purchheim, Germany), RFP (Rockland, Pottstown, PA, USA), Contactin-2 (AF1714 R&D system, Minneapolis, MN, USA), Pecam-1 (MEC13.3-BD Pharmingen, San Jose, CA, USA), HCN4 (Millipore, Burlington, MA, USA), ETV-1 (Abcam, Cambridge, U.K.), Troponin I (Abcam) and WGA-Cy3 (Sigma, St. Louis, MO, USA). Antibodies against Cx43 and CX40 are homemade and previously described [6 (link),23 (link)].

Choquet C., Sicard P., Vahdat J., Nguyen T.H., Kober F., Varlet I., Bernard M., Richard S., Kelly R.G., Lalevée N, & Miquerol L. (2023). Nkx2-5 Loss of Function in the His-Purkinje System Hampers Its Maturation and Leads to Mechanical Dysfunction. Journal of Cardiovascular Development and Disease, 10(5), 194.

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Western Blot Analysis of Cardiac Proteins

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Western blots were performed according to reported protocols [23] (link), [24] . Briefly, 50 μg of total proteins were loaded per lane, separated using 10% SDS-PAGE, and transferred to a nitrocellulose membrane. The membrane was blocked in 5% skim milk at room temperature for at least 2 h and then incubated in primary antibody overnight at 4 °C. After washing three times with TBST, membranes were incubated with the corresponding secondary antibody at room temperature for 2 h. Finally, the bands were visualised using an ECL kit (CW0049, CWBIO, Beijing, China). The primary antibodies in this article were used including: SERCA (ab2861, 1:1000), RyR2 (ab2868, 1:1000), NCX (ab177952, 1:1000), α1C (ab84814, 1:1000), calpain-2 (ab126600, 1:1000), STIM1 (ab57834, 1:1000), CaMKⅡ (ab22609, 1:1000), p-CaMKⅡ (ab32678, 1:1000), p-PLB (ab15000, 1:1000), calmodulin (ab45689, 1:1000), Troponin I (ab52862, 1:1000) and tubulin (ab6046, 1:2000) were purchased from abcam (Cambridge, UK); FKBP12.6 (sc-376135, 1:200) and PLB (sc-393990, 1:200) were purchased from Santa Cruz Biotechnology (California, USA); BAG3 (A14826, 1:500), α2δ (A10315, 1:500), γ (A10014, 1:500) and β (A9304, 1:500) were purchased from ABclonal (Wuhan, China). The secondary antibodies in this article were used including: rabbit (ab6721, 1:2000) and mouse (ab6728, 1:2000).

Wang R., Wang M., Zhou J., Dai Z., Sun G, & Sun X. (2020). Calenduloside E suppresses calcium overload by promoting the interaction between L-type calcium channels and Bcl2-associated athanogene 3 to alleviate myocardial ischemia/reperfusion injury. Journal of Advanced Research, 34, 173-186.

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Cardiac Tissue Histology and Staining

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Hearts were dehydrated in 30% sucrose solution, embedded in Tissue-Tek^® Optimal Cutting Temperature Compound (Sakura Finetek, Torrance, CA, USA), snap-frozen in liquid nitrogen, and cut into sections of thickness 5 μm for staining. Sections were washed with phosphate-buffered saline, permeabilized with 0.2% Triton X (Sigma–Aldrich) and blocked with 5% bovine serum albumin (Gibco, Billings, MT, USA). Apoptosis was evaluated with a terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) kit (Roche Applied Science, Basel, Switzerland); cell proliferation was incubated with ki67 (Abcam, United Kingdom) and ROSs was stained with dihydroethidium (DHE, Beyotime Biotechnology, China). Cardiomyocytes were stained with troponin I (Abcam, United Kingdom) and nuclei were counterstained with 4′,6-diamidino-2-phenylindole (DAPI; Vector Laboratories, Burlingame, CA, USA).

Zhang L., Wang Y., Li C., Shao C., Zhou H., Yang J., He Y, & Wan H. (2020). Dan Hong Injection Protects Against Cardiomyocytes Apoptosis by Maintaining Mitochondrial Integrity Through Keap1/Nuclear Factor Erythroid 2-Related Factor 2/JNK Pathway. Frontiers in Pharmacology, 11, 591197.

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Multimarker Immunofluorescence Imaging of Cardiac Tissue

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Tissue of the left ventricle (superficial and luminal layer) was also dewaxed and hydrated. ASs primary antibody, we used a rabbit anti-α-actinin (clone N1N3) (GeneTex, Ivine, CA, USA) and a mouse anti-desmin (GeneTex, Irvine, CA, USA). AS secondary antibody a goat anti-rabbit (AF-488) (Jackson Immuno research Laboratories, West Grove, PA, USA) as well as a goat anti-mouse (AF-647) (Jackson Immuno Research Laboratories, West Grove, PA, USA) antibody was used. We further stained the sections with an anti-Dystrophin (Abcam, Cambridge, UK) antibody, as well as a N-Cadherin-antibody (Abcam, Cambridge, UK). Further, B-Catenin (Abcam, Cambridge, UK) and Troponin I (Abcam, Cambridge, UK) were detected by staining. Counterstaining was conducted with Höchst 33342 (Sigma, Darmstadt, Germany). Following staining, sections were mounted with ProLong Gold Antifade Reagent (Invitrogen, Carlsbad, CA, USA). For quantification, the Axio ImagerM.1 microscope and the Zeiss AxioVision software 4.9 (Zeiss, Jena, Germany) was also used. Results are presented as mean density of each group (arbitrary units).

Weber B., Lackner I., Miclau T., Stulz J., Gebhard F., Pfeifer R., Cinelli P., Halvachizadeh S., Teuben M., Pape H.C., Lipiski M., Cesarovic N, & Kalbitz M. (2021). Early myocardial damage (EMD) and valvular dysfunction after femur fracture in pigs. Scientific Reports, 11, 8503.

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Immunofluorescence Analysis of Cardiac Markers

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Specific antigen binding was performed by incubating sections with the respective primary antibodies for α-actinin (GeneTex, Irvine, CA, USA), desmin (GeneTex, Irvine, CA, USA), troponin I (Abcam, Cambridge, UK), connexin43 (Cell Signalling Technology, Cambridge, UK), zonula occludens-1 (Bioss, Woburn, MA, USA), claudin-18 (ThermoFisher, Waltham, MA, USA), and occludin (Bioss, Woburn, MA, USA) overnight at 4°C. Specific antibody binding was detected by using either AlexaFluor488-labelled (Jackson ImmunoResearch, West Grove, PA, USA), rhodamine-labelled (Jackson ImmunoResearch, West Grove, PA, USA), or AlexaFluor647-labelled (Jackson ImmunoResearch, West Grove, PA, USA) secondary antibodies. Cell nuclei were counterstained with Hoechst. Sections were analysed by fluorescence microscopy by using an Axio Imager M.2 microscope and the Zeiss ZEN 2.3 software (Zeiss, Jena, Germany). Fluorescence intensities as well as the amount of apoptotic cells were evaluated using ImageJ software (National Institutes of Health, Bethesda, MD, USA). Results are presented as mean fluorescence intensity.

Lackner I., Weber B., Chakraborty S., Braumüller S., Huber-Lang M., Gebhard F, & Kalbitz M. (2020). Toll-Like Receptor-Mediated Cardiac Injury during Experimental Sepsis. Mediators of Inflammation, 2020, 6051983.

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Characterizing Subcellular Protein Localization

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Cells were fixed with 4% formaldehyde for 15 min at RT and permeabilized with 0.3% Triton-X for 10 min at RT. Unspecific binding sites were blocked with 10% goat serum, and specific antigen detection was performed by incubating cells with the respective primary antibodies for ryanodine receptor 1 (RyR1) (Abcam, Cambridge, UK), desmin (GeneTex, Irvine, CA, USA), and troponin I (Abcam, Cambridge, UK) for overnight at 4°C. Specific antibody binding was detected by using either AlexaFluor647-labelled (Jackson ImmunoResearch, West Grove, PA, USA) or rhodamine-labelled (Jackson ImmunoResearch, West Grove, PA, USA) secondary antibodies. Cell nuclei were stained with Hoechst. Fluorescence was investigated by fluorescence microscopy using an Axio Imager M.2 microscope and the Zeiss ZEN 2.3 software (Zeiss, Jena, Germany). Fluorescence intensities were evaluated using ImageJ software (National Institutes of Health, Bethesda, MD, USA). Values are illustrated as mean fluorescence intensity.

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