Log In Sign up
The largest database of trusted experimental protocols
> Anatomy > Cell Component > Sarcomeres

Sarcomeres

Sarcomeres are the fundamental contractile units of striated muscle fibers.
They are composed of a repeating pattern of thick and thin filaments that slide past each other during muscle contraction, generating force and movement.
Sarcomeres play a crucial role in the structure and function of skeletal, cardiac, and smooth muscles, and their study is essential for understanding musclular disfunction and disease.
This MeSH term provides a concise overview of the key features and importance of sarcomeres in biomedical research.

Most cited protocols related to «Sarcomeres»

1
Muscle Force Response to Length Change
Skinned muscle fiber bundles were attached to the arm of a displacement motor (model 308B; Aurora Scientific Inc.) on one end and to a force transducer (AE 801; Sensor One Technologies Corporation) on the other end using aluminum T-clips. Mounted bundles were placed in a 15-µl well, where they were bathed in either activating or relaxing solutions. Sarcomere length, SL, was measured by laser light diffraction methods. Visual display of the first-order laser light diffraction allowed judgment as to the accuracy of the SL assessment and the quality of the preparation. SL in all preparations was set to 2.2 µm before Ca2+ activation. Fiber bundle length at SL 2.2 µm was recorded as baseline muscle length (ML). Fiber bundle cross-sectional area was calculated from optical measurements of major and minor axes using an assumption of an elliptical cross section.
Ca2+-activated force was measured at maximal level of activation (pCa 4.3). The amount of free [Ca2+] in solution and corresponding pCa value was determined using methods described previously (Fabiato and Fabiato, 1979 (link)). Once steady-state isometric force was achieved, the length of the constantly activated muscle was commanded to change according to the following step length change protocol. A command was given to the motor for the muscle to increase its length by 0.5% of ML in a step-like fashion. This length was maintained for 5 s at which time the muscle was commanded to rapidly return to ML. After another 5 s, a command was given to increase muscle length to 1.0% of ML, which was held for 5 s before rapidly returning to ML. This procedure was repeated for additional step increases in muscle length of 1.5 and 2.0%. All step-like changes in muscle length were essentially completed in 1–2 ms. Measurements of force and muscle length were digitally sampled every 1 ms during the entire procedure. In all cases, force stabilized to a steady-state value within ∼1.5 s after a change in length. The first 1.5 s of the force response to the increase in muscle length was taken as a response to quick stretch, and the first 1.5 s of force response after the return of muscle length to ML was taken as a response to quick release. All force and muscle length records were normalized to their respective values just before length change.
Ford S.J., Chandra M., Mamidi R., Dong W, & Campbell K.B. (2010). Model representation of the nonlinear step response in cardiac muscle. The Journal of General Physiology, 136(2), 159-177.
Publication 2010
Aluminum ARID1A protein, human Clip Epistropheus Fibrosis Light MS 1-2 Muscle Tissue Sarcomeres Transducers
2
Genetic Variants Associated with HCM
322 HCM patients and 852 healthy volunteers (both confirmed by cardiac MRI) recruited to the NIHR Royal Brompton cardiovascular BRU were sequenced using the IlluminaTruSight Cardio Sequencing Kit13 (link) on Illumina MiSeq and NextSeq platforms. This study had ethical approval (REC: 09/H0504/104+5) and informed consent was obtained for all subjects. The number of rare variants in the eight sarcomeric genes associated with HCM (MYBPC3, MYH7, TNNT2, TNNI3, MYL2, MYL3, TPM1 and ACTC1) were calculated for all protein altering variants (frameshift, nonsense, splice donor/acceptor, missense and in-frame insertions/deletions), with case/control odds ratios calculated separately for non-overlapping ExAC AF bins with the following breakpoints: 4x10−5, 1x10−4, 5x10−4 and 1x10−3. Odds Ratios were calculated as OR=(cases with variant/cases without variant)/(controls with variant/controls without variant).
Whiffin N., Minikel E., Walsh R., O’Donnell-Luria A.H., Karczewski K., Ing A.Y., Barton P.J., Funke B., Cook S.A., MacArthur D, & Ware J.S. (2017). Using high-resolution variant frequencies to empower clinical genome interpretation. Genetics in Medicine, 19(10), 1151-1158.
Publication 2017
Cardiovascular System Frameshift Mutation Genes Healthy Volunteers Heart INDEL Mutation Mutant Proteins Mutation, Nonsense Patients Reading Frames Sarcomeres Tissue Donors
3
Cardiac Function in Nox2 Transgenic Mice

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2015
Animals Biological Assay Caffeine Calcium calyculin A Chemiluminescence DNA, Complementary Homo sapiens Left Ventricles Lucigenin malachite green Mice, Laboratory Mice, Transgenic Myocardium Myocytes, Cardiac myosin light chain 2 Pressure Protein Phosphatase Psychological Inhibition Sarcomeres Sodium Student Systole Transients
4
Drosophila Genetic Toolkit for Developmental Biology
Drosophila stocks used included apME-NLS::dsRed4, Df(3L)GN3426, ensHP36480 (Bloomington), ensf07121 (Harvard), Df-ensΔ3277, ensΔN, ensΔC (ref. 8 (link)), khc8, khc4, khc23 (ref. 10 (link)), klc8ex94 (ref. 27 (link)), twi-Gal44, alpha-Gal4, G7-Gal428 (from K. Broadie), and UAS-ens-IR lines 106207 and 18491 (VDRC). UAS-ensHA transgenic flies were generated by BestGene Inc. Mouse cells were transfected with siRNA using lipofectamine RNAiMAX (Invitrogen) or DNA using lipofectamine 2000 (Invitrogen). Primary antibodies used were: rabbit anti-dsRed (Clontech), rat anti-tropomyosin (Abcam), mouse anti-myosin heavy chain (from S. Abmayr), rabbit anti-Zasp (from F. Schöck), chicken anti-βgal (Abcam), mouse anti-α-Tubulin (Sigma), rat anti-Ensconsin (from P. Rørth), guinea pig anti-Krüppel (from J. Reinitz), rabbit anti-Eve (from M. Frasch), mouse anti-βPS Integrin (DSHB), rabbit anti-Vestigial (from S. Carroll), FITC conjugated anti-HRP (Jackson ImmunoResearch), mouse anti-Discs large (DSHB), rabbit anti-ATP synthase29 (link) (from H. Duan), rat anti-DE-Cadherin (DSHB), mouse anti-Chaoptin 24B10 (DSHB), rat anti-Elav (DSHB), Alexa Fluor 488 conjugated wheat germ agglutinin (Invitrogen), MF20 (DSHB), rabbit anti-KHC (Santa Cruz), mouse anti-c-Myc (Roche), rabbit anti-GFP (Invitrogen). Secondary antibodies were either biotinylated (Vector Laboratories and Jackson ImmunoResearch) or conjugated to Alexa Fluor 488, 555, or 647. The fusion index30 (link), sarcomere length15 (link), bouton number17 (link), and larval velocity14 (link) were quantified as described with minor modifications (see methods). The yeast 2-hybrid was performed with full length Ens by Hybrigenics S.A Services using a 0–24 hour Drosophila cDNA library. Standard protocols were used for immunoprecipitation, western blot, and qPCR experiments and are described in Methods.
Metzger T., Gache V., Xu M., Cadot B., Folker E.S., Richardson B.E., Gomes E.R, & Baylies M.K. (2012). MAP and Kinesin dependent nuclear positioning is required for skeletal muscle function. Nature, 484(7392), 120-124.
Publication 2012
alexa fluor 488 alpha-Tubulin Animals, Transgenic Antibodies Cadherins Cavia porcellus cDNA Library Cells Chickens Cloning Vectors Diptera Drosophila E MAP 115 Fluorescein-5-isothiocyanate Hybrids Immunoprecipitation Integrins Larva Lipofectamine lipofectamine 2000 Mice, House Myosin Heavy Chains Rabbits RNA, Small Interfering Sarcomeres Tropomyosin Western Blotting Wheat Germ Agglutinins Yeast, Dried
5
High-Resolution Separation of Cardiac Titin Isoforms
Gel electrophoresis has been used extensively to determine the size and quantity of proteins. Muscle tissues such as cardiac and skeletal commonly express a variety of giant proteins (larger than 0.5 MDa), which play important roles in muscle structure and function. Titin, also called connectin, is the largest known sarcomere protein. In the sarcomere, titin plays a critical role in maintaining structural integrity and developing passive tension with stretch [1] (link). Titin can thus be viewed as a molecular spring in striated muscle. Titin gene undergoes alternative splicing, and generates numerous isoforms in the heart [2] (link). The size of different titin isoforms ranges from ∼3 to 4.2 MDa (theoretically 4.2 MDa is full size only when all exons are expressed which has never been detected by SDS-agarose gel so far) in the heart [3] (link). Titin N2B isoform is produced from a single splicing pathway with a size of approximately 3.0 MDa. N2BA isoforms are produced from multiple splicing pathways, and detectable N2BA isoforms are N2BA-A1 (adult form), A2 (adult form), N1 (embryonic and neonatal form) and N2 (embryonic and neonatal form) with sizes of about 3.4, 3.2, 3.7 and 3.6 MDa respectively [2] (link), [4] . Recently, it has been reported that titin gene splicing is mainly regulated by RNA binding protein 20 (RBM20). In RBM20 knockout rat heart, a new N2BA isoform named N2BA-G with a size of approximately 3.9 MDa has only been expressed [5] (link). Cardiac titin isoforms alteration has been identified and associated with human heart failure [6] (link), [7] (link). Gel electrophoresis is the simplest and most direct way to observe the alteration of titin isoforms during developmental and pathological changes. However, electrophoretic analysis of large proteins has been difficult to separate titin isoform proteins. In order to clearly and easily resolve various titin isoforms, SDS-agarose gels have been developed [8] (link). The present vertical SDS-agarose gel electrophoresis system has been modified and used as an efficient method for high-resolution separation of titin isoforms.
Zhu C, & Guo W. (2017). Detection and quantification of the giant protein titin by SDS-agarose gel electrophoresis. MethodsX, 4, 320-327.
Publication 2017
Adult Connectin Electrophoresis Electrophoresis, Agar Gel Embryo Exons Gels Genes Gigantism Heart Heart Failure Homo sapiens IFIH1 protein, human Infant, Newborn Muscle, Striated Muscle Tissue Myocardium Protein Isoforms Proteins RNA-Binding Proteins Sarcomeres SDCBP protein, human Sepharose Skeleton Staphylococcal Protein A Titin Kinase

Most recents protocols related to «Sarcomeres»

1
Immunofluorescent Characterization of iPSC-Derived Cardiomyocytes
IPSc-derived cardiomyocytes were cultured on glass slides coated with Synthemax II-SC (Corning) in RPMI-1640/B-27 with Y27632 (5 μM) media for 2 days. Cells were fixed with 4% formaldehyde for 15 min at room temperature. Fixed cells were blocked in antibody buffer (5% BSA, 0.1% Tween-20 in PBS) for 1 h at room temperature. Following blocking, cells were incubated overnight at 4 °C with cardiac troponin-T antibody (abcam, ab45932, 1:200), α-Actinin antibody (Sigma, A7811, 1:800), and/or Connexin 43 (Cell Signaling Technology, 1:100) in antibody buffer. After the overnight incubation, cells were washed three times in antibody buffer. Following washing, cells were incubated with Alexa-Fluor conjugated secondary antibodies (Thermo Fisher Scientific, Alexa 488 Donkey anti-Rabbit IgG and Alexa 594 Goat anti-Ms IgG1) at a 1:1,000 dilution in antibody buffer for 1 h at room temperature. Nuclei were stained by DAPI at 1 μg/ml and Wheat Germ Agglutinin (Thermo Fisher Scientific, W21404) was used to stain cell membrane for 10 min at room temperature in antibody buffer. Following washing in PBS to remove unbound complexes, sarcomeres were analyzed using a Zeiss LSM510 confocal microscope. Images were processed with Zeiss software (Axiovision Rel4.8 and Zen Blue). Circularity measurements were made by comparing cardiomyocyte length to width and were expressed as a circularity index whereby circularity index = width/length15 (link). Sarcomere distance measurements were made with ImageJ15 (link). All measurements were made with a double-blinding method.
Hsueh Y.C., Pratt R.E., Dzau V.J, & Hodgkinson C.P. (2023). Novel method of differentiating human induced pluripotent stem cells to mature cardiomyocytes via Sfrp2. Scientific Reports, 13, 3920.
Publication 2023
Actinin Alexa594 anti-IgG Antibodies Buffers Cardiac Arrest Cell Nucleus DAPI Equus asinus Formaldehyde GJA1 protein, human Goat Heart IgG1 Immunoglobulins Induced Pluripotent Stem Cells Microscopy, Confocal Myocytes, Cardiac Plasma Membrane Rabbits Sarcomeres Stains Technique, Dilution Troponin T Tween 20 Wheat Germ Agglutinins Y 27632
2
Sarcomere Alignment Quantification
We used a Sarcomere Organization Texture Analysis algorithm that uses Haralick texture structures to quantify sarcomere alignment as previously described (37 (link)).
Lin Z., Garbern J.C., Liu R., Li Q., Mancheño Juncosa E., Elwell H.L., Sokol M., Aoyama J., Deumer U.S., Hsiao E., Sheng H., Lee R.T, & Liu J. (2023). Tissue-embedded stretchable nanoelectronics reveal endothelial cell–mediated electrical maturation of human 3D cardiac microtissues. Science Advances, 9(10), eade8513.
Publication 2023
Sarcomeres
3
Quantitative PCR Analysis of RNA from Treated NRVMs
Total RNA was extracted from NRVMs seeded at 1.0 × 106 cells/well after appropriate treatments as indicated in the main text (e.g., 24-h PE treatment ± TMG/OSMI-1 treatment). The treated cells were washed with ice-cold PBS (3×) and RNA was extracted with the RNeasy kit (Cat. No. 74704, Qiagen), including a proteinase K digestion step to remove abundant sarcomeric proteins. In-column DNaseI treatment (Cat. No. 79254, Qiagen) was used to digest away genomic DNA. For reverse transcription, we used a QuantiTect reverse transcription kit (Cat. No. 205311, Qiagen) and an input of 850 ng of total RNA. To control for potentially residual genomic DNA carry-over, reactions without reverse-transcriptase were set up in parallel. Real-time quantitative PCR was performed with the Power SYBR Green master mix (Cat. No. 4367659, Thermo Fisher Scientific) in the presence of 500 nM forward and reverse primers (for gene-specific sequences see Table S2). A total of 45 cycles of amplification were done (15 s at 95 °C for melting followed by 30 s at 60 °C for annealing and elongation) using the CFX384 Touch system (Bio-Rad). Each sample was run in technical triplicates. Gene expression was quantified with the ΔCt method using Gapdh and 36B4 as housekeeping genes.
Papanicolaou K.N., Jung J., Ashok D., Zhang W., Modaressanavi A., Avila E., Foster D.B., Zachara N.E, & O'Rourke B. (2023). Inhibiting O-GlcNAcylation impacts p38 and Erk1/2 signaling and perturbs cardiomyocyte hypertrophy. The Journal of Biological Chemistry, 299(3), 102907.
Publication 2023
Cells Common Cold Digestion Endopeptidase K GAPDH protein, human Gene Expression Genes Genes, Housekeeping Genome Oligonucleotide Primers Proteins Real-Time Polymerase Chain Reaction Reverse Transcription RNA-Directed DNA Polymerase Sarcomeres SYBR Green I Touch
4
Cardiac Differentiation of hiPSCs
Two different batches of hiPSC-CMs were used for this study, a commercial one (Pluricyte® CMs provided by Ncardia, Gosselies, Belgium) and a laboratory handle one. The latter was produced by directed cardiac differentiation of previously generated control hiPSCs.29 (link),56 (link),57 (link)
In brief, cardiac induction and generation of hiPSC-CMs were obtained as previously reported, using a chemically-defined serum-free protocol, which is based on activation (CHIR99021) and inhibition (IWR1) of the Wnt pathway in RPMI-B27 medium.58 (link),59 (link),60 (link) In this work, CMs were differentiated from two different control iPSC lines (one male and one female) between the 18th and the 35th passage in culture. Importantly, employed cell lines were regularly tested for being free of major chromosomal abnormalities by karyotype analysis. CMs were used for the experiments 25–30 days after spontaneous contracting activity was started, a differentiation stage at which they expressed the repertoire of sarcomeric proteins, calcium regulators, and ionic channels necessary for their correct functionality. Purity of differentiated CM populations was regularly checked before each experiment to be greater than 90% (not shown). The commercial batch was thawed and cultured following the manufacturer’s protocol. In terms of plating density, cells for both batches were seeded onto the material at a confluence comprised between 50% and 60% on fibronectin coated (15 μg/ml in PBS buffer solution) 18-mm round glass coverslip (VWR, Radnor, USA). The cells were maintained in incubator at 37°C and 5% CO2.
Vurro V., Federici B., Ronchi C., Florindi C., Sesti V., Crasto S., Maniezzi C., Galli C., Antognazza M.R., Bertarelli C., Di Pasquale E., Lanzani G, & Lodola F. (2023). Optical modulation of excitation-contraction coupling in human-induced pluripotent stem cell-derived cardiomyocytes. iScience, 26(3), 106121.
Publication 2023
Buffers Calcium Cell Lines Cells Chir 99021 Chromosome Aberrations Females Fibronectins Heart Human Induced Pluripotent Stem Cells Induced Pluripotent Stem Cells Ion Channel Karyotyping Males Population Group Proteins Psychological Inhibition Sarcomeres Serum Wnt Signaling Pathway
5
Quantifying Cardiomyocyte Alignment and Contractility
Sarcomere energetics was assessed in Triton permeabilized strips of mutant and donor ventricular samples.6 (link) To exclude myocardial disarray as an artificial contributor to mechanical and energetic data, we employed a novel method able to quantify myocyte alignment, disarray, and contractile tissue content in tissue strips.22 (link) The local cardiomyocyte’s orientation was detected with cellular resolution and represented as 3D vectors. Global Alignment quantifies the average alignment degree of the cells along the longitudinal axis of the preparation (Y), while local disarray quantifies the misalignment degree of nearby orientation vectors with respect to the mean local direction of the cells. The percentage of contractile tissue in the preparation is quantified as the ratio between the effective volume of labeled tissue (ie, total volume of cardiomyocytes thanks to the high-specificity of anti-α-actinin antibody staining) and the total volume of the preparation.
Pioner J.M., Vitale G., Steczina S., Langione M., Margara F., Santini L., Giardini F., Lazzeri E., Piroddi N., Scellini B., Palandri C., Schuldt M., Spinelli V., Girolami F., Mazzarotto F., van der Velden J., Cerbai E., Tesi C., Olivotto I., Bueno-Orovio A., Sacconi L., Coppini R., Ferrantini C., Regnier M, & Poggesi C. (2023). Slower Calcium Handling Balances Faster Cross-Bridge Cycling in Human MYBPC3 HCM. Circulation Research, 132(5), 628-644.
Publication 2023
Actinin Antibody Specificity Cells Cloning Vectors Epistropheus Heart Ventricle Muscle Cells Muscle Contraction Myocardium Myocytes, Cardiac Sarcomeres Tissue Donors Tissues

Top products related to «Sarcomeres»

1
4 6 diamidino 2 phenylindole (dapi) by Thermo Fisher Scientific
Sourced in United States, Germany, United Kingdom, Japan, China, Canada, Italy, Australia, France, Switzerland, Spain, Belgium, Denmark, Panama, Poland, Singapore, Austria, Morocco, Netherlands, Sweden, Argentina, India, Finland, Pakistan, Cameroon, New Zealand
DAPI is a fluorescent dye used in microscopy and flow cytometry to stain cell nuclei. It binds strongly to the minor groove of double-stranded DNA, emitting blue fluorescence when excited by ultraviolet light.
2
Sarcomeric α actinin by Merck Group
Sourced in United States
Sarcomeric α-actinin is a structural protein found in the z-discs of striated muscle cells. It plays a crucial role in the organization and stabilization of the actin filaments within the sarcomeres, which are the basic contractile units of muscle fibers. This protein is an important component of the cytoskeleton and is essential for the proper functioning and maintenance of muscle tissue.
3
Triton x 100 by Merck Group
Sourced in United States, Germany, United Kingdom, Italy, China, Japan, France, Canada, Sao Tome and Principe, Switzerland, Macao, Poland, Spain, Australia, India, Belgium, Israel, Sweden, Ireland, Denmark, Brazil, Portugal, Panama, Netherlands, Hungary, Czechia, Austria, Norway, Slovakia, Singapore, Argentina, Mexico, Senegal
Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
4
4 6 diamidino 2 phenylindole (dapi) by Merck Group
Sourced in United States, Germany, Japan, United Kingdom, China, Italy, Sao Tome and Principe, France, Macao, Canada, Switzerland, Spain, Australia, Denmark, India, Poland, Israel, Belgium, Sweden, Ireland, Netherlands, Panama, Brazil, Portugal, Czechia, Puerto Rico, Austria, Hong Kong, Singapore
DAPI is a fluorescent dye that binds strongly to adenine-thymine (A-T) rich regions in DNA. It is commonly used as a nuclear counterstain in fluorescence microscopy to visualize and locate cell nuclei.
5
Alexa fluor 488 by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, Japan, France, Italy, Canada, China, Spain, Switzerland, Denmark, Australia, Hungary, Belgium, Ireland, Israel, Netherlands, Moldova, Republic of, India, Austria, Czechia, Poland
Alexa Fluor 488 is a fluorescent dye used in various biotechnological applications. It has an excitation maximum at 495 nm and an emission maximum at 519 nm, producing a green fluorescent signal. Alexa Fluor 488 is known for its brightness, photostability, and pH-insensitivity, making it a popular choice for labeling biomolecules in biological research.
6
Ab9465 by Abcam
Sourced in United States, United Kingdom
Ab9465 is a mouse monoclonal antibody specific for human GAPDH. GAPDH is a glycolytic enzyme involved in energy production. The antibody can be used for the detection of GAPDH in various applications.
7
Fura 2 am by Thermo Fisher Scientific
Sourced in United States, United Kingdom, Germany, Italy, France, Spain, Australia, Japan, China, Canada, Belgium, Austria, Hungary, Macao
Fura-2 AM is a fluorescent calcium indicator used for measuring intracellular calcium levels. It is a cell-permeable derivative of the parent compound Fura-2. Fura-2 AM can be loaded into cells, where intracellular esterases cleave off the acetoxymethyl (AM) ester group, trapping the Fura-2 indicator inside the cell.
8
Ionwizard software by IonOptix
Sourced in United States
IonWizard is a software package designed for the acquisition, analysis, and presentation of data from IonOptix's line of lab equipment. It provides a user-friendly interface for recording and processing measurements related to cellular ion dynamics.
9
A7811 by Merck Group
Sourced in United States, United Kingdom
The A7811 is a laboratory equipment product from the Merck Group. It is designed for general laboratory use. The core function of the A7811 is to perform specific tasks within a laboratory setting. No further details on the intended use or features of this product can be provided in an unbiased and factual manner.
10
Bovine serum albumin (bsa) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Japan, France, Sao Tome and Principe, Canada, Macao, Spain, Switzerland, Australia, India, Israel, Belgium, Poland, Sweden, Denmark, Ireland, Hungary, Netherlands, Czechia, Brazil, Austria, Singapore, Portugal, Panama, Chile, Senegal, Morocco, Slovenia, New Zealand, Finland, Thailand, Uruguay, Argentina, Saudi Arabia, Romania, Greece, Mexico
Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.

More about "Sarcomeres"

Sarcomeres are the fundamental contractile units that make up striated muscle fibers, such as those found in skeletal, cardiac, and smooth muscles.
These repeating patterns of thick and thin filaments are responsible for the sliding motion that generates force and movement during muscle contraction.
Understanding the structure and function of sarcomeres is crucial for studying muscular dysfunction and disease.
Key aspects of sarcomeres include their composition, with thick myosin filaments and thin actin filaments that slide past each other, as well as the role of proteins like sarcomeric α-actinin in anchoring and organizing these filaments.
Techniques like immunofluorescence using DAPI, Alexa Fluor 488, and Ab9465 antibodies can be used to visualize and study the sarcomeric structure.
Sarcomere research also involves the use of various tools and reagents, such as the detergent Triton X-100 for permeabilization, the calcium-sensitive dye Fura-2 AM for measuring intracellular calcium dynamics, and the IonWizard software for analyzing muscle fiber contractility.
Compounds like A7811 can also be used to investigate sarcomere function and its role in muscular disorders.
By leveraging the insights gained from the study of sarcomeres, researchers can gain a deeper understanding of the mechanisms underlying muscle contraction and develop new strategies for addressing muscular dysfunctions and diseases.
Whether you're studying skeletal, cardiac, or smooth muscle, the complex yet fascinating world of sarcomeres holds the key to unlocking important biomedical discoveries.