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.
Muscle, Striated
Striated muscle is a type of skeletal muscle tissue characterized by its distinctive banded appearance under a microscope.
These muscle fibers are composed of repeating contractile units called sarcomeres, which allow for rapid, coordinated movement.
Striated muscle is found in the skeletal muscles that attach to bones and facilitate locomotion, as well as in the cardiac muscle of the heart.
Understanding the structure and function of striated muscle is crucial for research in areas such as exercise physiology, neuromuscular disorders, and regenerative medicine.
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These muscle fibers are composed of repeating contractile units called sarcomeres, which allow for rapid, coordinated movement.
Striated muscle is found in the skeletal muscles that attach to bones and facilitate locomotion, as well as in the cardiac muscle of the heart.
Understanding the structure and function of striated muscle is crucial for research in areas such as exercise physiology, neuromuscular disorders, and regenerative medicine.
Optimize your research on striated muscle with the power of PubCompare.ai's AI-driven platform, which can help you discover the best protocols and products from literature, pre-prints, and patents through intelligent comparisons.
Empowher yourself to make informed decisions and accelerate your discoveries in this important field of study.
Most cited protocols related to «Muscle, Striated»
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
The bases encoding amino acids 3402–3675 (corresponding to exons 71–78) were deleted from the full length murine dystrophin cDNA (sequence data available from EMBL/GenBank/DDBJ under accession No. M68859) by recombinant PCR, leaving the last three amino acids (exon 79) of the dystrophin protein unaltered. This dystrophin Δ71–78 cDNA was cloned into an expression vector containing bases −2139 to +239 of the human α-skeletal actin (HSA) promoter (Brennan and Hardeman 1993 ). A splice acceptor from the SV40 VP1 intron (isolated as a 400 bp HindIII/XbaI fragment from pSVL; Amersham Pharmacia Biotech) was inserted immediately 3′ of the HSA fragment, and the SV40 polyadenylation signal (isolated as a BamHI fragment from pCMVβ; MacGregor and Caskey 1989 ) was inserted 3′ of the dystrophin cDNA. The excised dystrophin Δ71–78 expression cassette was injected into wild-type C57Bl/10 × SJL/J F2 hybrid embryos, and F0 mice were screened by PCR. Five positive F0's were backcrossed onto the C57Bl/10mdx background, and most further studies focused on the line with the most uniform expression levels. Some studies used previously described transgenic mdx mice that express dystrophin constructs deleted approximately for exons 71–74 (Δ71–74) or exons 75–78 (Δ75–78), which remove amino acids 3402–3511 and 3528–3675, respectively (Rafael et al. 1996 ). Transgenic mdx line Dp71 expresses the Dp71 isoform of dystrophin in striated muscle (Cox et al. 1994 ).
Actins
Amino Acids
Animals, Transgenic
BP 400
Cloning Vectors
DMD protein, human
DNA, Complementary
Embryo
Exons
Homo sapiens
Hybrids
Introns
Mice, Inbred mdx
Mice, Laboratory
Mice, Transgenic
Mus
Muscle, Striated
Polyadenylation
Protein Isoforms
Proteins
Simian virus 40
Skeleton
A fresh sample of a soft tissue sarcoma which had grown in striated muscle of a patient was obtained and transported immediately to the laboratory at AntiCancer, Inc., on wet ice. The sample was cut into 5-mm fragments and implanted subcutaneously in nude mice. After three weeks, the subcutaneously-implanted tumors grew to more than 10 mm in diameter. The subcutaneously-grown tumors were then harvested and cut into small fragments (3 mm3). After the mice were anesthetized with the ketamine solution described above, a 5-mm skin incision was made on the right high thigh into the biceps femoris, which was split to make space for the sarcoma tissue fragment. A single tumor fragment was implanted orthotopically into the space to establish the PDOX model. The wound was closed with a 6-0 nylon suture (Ethilon, Ethicon, Inc., NJ, USA).
Biceps Femoris
Ethilon
Ketamine
Mice, Nude
Mus
Muscle, Striated
Neoplasms
nylon 6
Patients
Sarcoma
Skin
Sutures
Thigh
Tissues
Wounds
The following autoantibodies were tested: anti-thyroid, anti-parietal cell, anti-gliadin, intrinsic factor blocking antibody, anti-islet cell, ANA, anti-cardiolipin, anti-RNP, anti-SSA/SSB, anti-SM, anti-striated, anti-smooth muscle, anti-microsomal, anti-mitochondrial, anti-acetylcholine receptor, anti-GM1, hepatitis B/C, HIV, HTLV-I and CMV. Immunoglobulin and complement levels were also tested.
Anti-GAD antibodies were initially tested in all patients and serially thereafter, in the 32 patients enrolled in the longitudinal protocol, by radioimmunoassay (RIA) using a commercial kit (Kronus, ID). Lumbar puncture was performed in 48 patients but CSF could not be obtained from 5 due to severe lumbar stiffness. CSF was examined for GAD antibodies, total immunoglobulins, oligoclonal bands, IgG index and intrathecal GAD-specific IgG synthesis, as previously described [6 (link), 25 (link), 26 (link)]. Anti-GAD antibodies were also measured in serial CSF’s (first and 2-year visits) in 10 patients by ELISA (Euroimmune, Lubeck). In 50 patients, sera were also tested for anti-glycine receptor and anti-GABAA antibodies using in-house cell-based immunofluorescent assays on live cells (cDNA clones kindly provided by Prof. A. Vincent, Oxford and Prof. J. Dalmau, Barcelona), as described [27 ].
Anti-GAD antibodies were initially tested in all patients and serially thereafter, in the 32 patients enrolled in the longitudinal protocol, by radioimmunoassay (RIA) using a commercial kit (Kronus, ID). Lumbar puncture was performed in 48 patients but CSF could not be obtained from 5 due to severe lumbar stiffness. CSF was examined for GAD antibodies, total immunoglobulins, oligoclonal bands, IgG index and intrathecal GAD-specific IgG synthesis, as previously described [6 (link), 25 (link), 26 (link)]. Anti-GAD antibodies were also measured in serial CSF’s (first and 2-year visits) in 10 patients by ELISA (Euroimmune, Lubeck). In 50 patients, sera were also tested for anti-glycine receptor and anti-GABAA antibodies using in-house cell-based immunofluorescent assays on live cells (cDNA clones kindly provided by Prof. A. Vincent, Oxford and Prof. J. Dalmau, Barcelona), as described [27 ].
Anabolism
Anti-Antibodies
Antibodies
Antibodies, Blocking
Autoantibodies
Cardiolipins
Cells
Cholinergic Receptors
Clone Cells
DNA, Complementary
Enzyme-Linked Immunosorbent Assay
Gliadin
Glycine Receptors
Hepatitis C virus
Human T-lymphotropic virus 1
Immunofluorescence
Immunoglobulins
Immunoglobulins, Oligoclonal
Intrinsic Factor
Islets of Langerhans
Lumbar Region
Microsomes
Mitochondria
Muscle, Striated
Parietal Cells, Gastric
Patients
Punctures, Lumbar
Serum
Thyroid Gland
alpha-Tropomyosin
Amino Acids
Chickens
Head
Homo sapiens
Leucine Zippers
Methionine
Microtubule-Associated Proteins
Muscle, Striated
Protein Isoforms
Smooth Muscles
Tail
Tropomyosin
XRCC4 protein, human
Most recents protocols related to «Muscle, Striated»
To estimate the genetic predisposition of AF, we constructed a polygenic risk score for each participant, which was derived from the current optimal genetic risk variant list from the meta-analyses excluding the UK Biobank participants (n=165 SNPs, Additional file 1 : Text S3, and Table S1) [15 (link)]. Briefly, most of the genome-wide significant risk variants for AF fall in genes that cause serious heart defects in humans (e.g., PITX2, TBX5) or near genes important for striated muscle function and integrity (e.g., CFL2, MYH7), which are crucial for the function of cardiac ion channels and calcium signaling. According to the number of risk alleles, we used imputed data to calculate the PRS through multiplying by the regression coefficient obtained from the previous study [23 (link)]: PRS = (β1 × SNP1 + β2 × SNP2 + … + β165 × SNP165). Furthermore, we classified each participant into three categories: low (lowest quartile), intermediate (mid two quartiles), and high (highest quartile) genetic AF risk groups.
Alleles
Birth
Congenital Heart Defects
Genes
Genetic Diversity
Genetic Predisposition to Disease
Genome
Heart
Homo sapiens
Ion Channel
Muscle, Striated
Population at Risk
Single Nucleotide Polymorphism
Protocol full text hidden due to copyright restrictions
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Animals
Capsid Proteins
Cellular Structures
Cloning Vectors
Dissection
Echocardiography
Euthanasia
Females
Freezing
Genome
Genotype
Heart
Institutional Animal Care and Use Committees
Joint Dislocations
Males
Mice, House
Muscle, Striated
Neck
Neoplasms
Nitrogen
Normal Saline
Strains
Tail
Tibia
Tissues
Veins
Muscle birefringence was analyzed by placing anesthetized larvae mounted in 2% methylcellulose in H2O on a glass polarizing filter and covering them with a second polarizing filter on a Leica M165 FC microscope. Larvae were photographed with a Nikon DS-Fi2 digital camera in bright field. The top filter was twisted to see the light refracting through striated muscle. Pixel intensity in the trunk region was measured with ImageJ software. Values were normalized for the sample area. Birefringence analysis was performed on sibling larvae and was followed by genotyping.
Birefringence
Larva
Light
Methylcellulose
Microscopy
Muscle, Striated
Muscle Tissue
Myo/Nog cells were identified in tissue sections by double labeling with the anti-BAI1 G8 IgM mouse mAb30 (link) and the anti-noggin goat polyclonal anti-serum (AF719; R&D Systems, Minneapolis, MN, USA), as described previously.25 (link),30 (link) Double labeling also was carried out with the IgM BAI1 mAb and IgG mAb antibodies to α-SMA (F3777 diluted 1:250; Sigma-Aldrich, St. Louis, MO, USA), striated muscle myosin II (ab58899 diluted 1:200; Abcam, Cambridge, MA, USA), the leukocyte markers CD68 (ab201340 diluted 1:200; Abcam), CD45 (ab10558 diluted 1:200; Abcam), and CD18 (MA1819 diluted 1:100; ThermoFisher Scientific, Waltham, PA, USA), and human nucleoli (ab190710 diluted 1:100; Abcam). The α-SMA mAb was directly conjugated with fluorescein. Other primary antibodies were visualized with AffiniPure Fab fragment subclass and species-specific secondary antibodies conjugated with Rhodamine Red or Alexa 488 (Jackson ImmunoResearch Laboratories, Inc., West Grove, PA, USA). The level of background fluorescence was determined by incubating sections in secondary antibody only. Apoptotic cells were identified with fluorescent terminal deoxynucleotidyl transferase–dUTP nick-end labeling (TUNEL) reagents (Roche Diagnostics, Mannheim, Germany). Coverslips were applied with Dapi Fluoro-Gel II Mounting Medium (Electron Microscopy Sciences, Hatfield, PA, USA).
Tissues were analyzed with the Nikon Eclipse E800 epifluorescence microscope (Nikon Instruments Inc., Melville, NY, USA) equipped with 10 x, 60 x, and 100 x lenses, the Infinity 3S camera (Teledyne DALSA, Waterloo, Ontario, Canada) and Image Pro Plus image analysis software program (Media Cybernetics, Rockville, MD, USA) and the Olympus Confocal Fluoview 1000 microscope equipped with a 60 x oil immersion lens and Fluoview software program (Olympus Corp., Tokyo, Japan). Adobe Photoshop version 23 (Adobe Inc., San Jose, CA, USA) was used to adjust photographs for brightness and contrast, and assembly and annotation of figures.
Tissues were analyzed with the Nikon Eclipse E800 epifluorescence microscope (Nikon Instruments Inc., Melville, NY, USA) equipped with 10 x, 60 x, and 100 x lenses, the Infinity 3S camera (Teledyne DALSA, Waterloo, Ontario, Canada) and Image Pro Plus image analysis software program (Media Cybernetics, Rockville, MD, USA) and the Olympus Confocal Fluoview 1000 microscope equipped with a 60 x oil immersion lens and Fluoview software program (Olympus Corp., Tokyo, Japan). Adobe Photoshop version 23 (Adobe Inc., San Jose, CA, USA) was used to adjust photographs for brightness and contrast, and assembly and annotation of figures.
anti-IgM
Antibodies
Apoptosis
Cell Nucleolus
Cells
DAPI
deoxyuridine triphosphate
Diagnosis
DNA Nucleotidylexotransferase
Electron Microscopy
Fluorescein
Fluorescence
Goat
Homo sapiens
Immunoglobulin G
Immunoglobulins
Immunoglobulins, Fab
Lens, Crystalline
Leukocytes
Microscopy
Microscopy, Confocal
Mus
Muscle, Striated
Myosin Type II
noggin protein
Rhodamine
Serum
Submersion
Tissues
The liver, gallbladder, kidney, urinary bladder, spleen, lung, pancreas, striated muscle (quadriceps femoris), and heart were removed immediately after the experimental procedure. Each organ or tissue specimen was divided into two and fixed overnight in 10% neutral buffered formaldehyde or 2.5% buffered glutaraldehid solutions (Sigma-Aldrich) for LM and transmission electron microscopy (TEM) analyses, respectively. Care was taken to obtain the samples from the fixed parts of the organs or tissues each time, i.e. kidney and heart samples were cross-sectioned through their mid-portion. The cortex and medulla containing kidney sections were evaluated. The organ or tissue samples were fixed in 10% phosphate buffered formalin (pH 7.0) at room temperature, rinsed in buffer, and dehydrated in graded series of ethanol before embedding in paraffin by using an automated tissue processor with constant vacuum. Five to seven micrometer thick sections were prepared with a sliding microtome (Leica). Hematoxylin and eosin and Masson trichrome (MT) stained sections (at least 10 sections per specimen) were examined by at least two independent investigators with a Leica DMR microscope. The images were captured via Leica DC500 digital camera and semi-quantitatively evaluated by using Leica application suite (LAS) software. An experienced histologist unaware of the grouping performed the semi-quantitative analysis by grading each parameter between 0 and 3; this procedure was devised as a modification of the one adopted in the study of Akıncı et al. [13 ]. In brief, four parameters (pulmonary edema, parenchymal congestion, alveolar hemorrhage, and peribronchial–perivascular–interstitial inflammation) were evaluated for the lung (the total maximum score is 12). Five parameters (necrosis, congestion, hepatocellular injury, periportal inflammation, and vacuolar degeneration) were evaluated for the liver (the total maximal score is 15). Two parameters (congestion and fibrosis) were evaluated for the spleen damage (the total maximum score is 6). Two parameters (congestion and necrosis) were evaluated for the kidney damage (the total maximum score is 6). Three parameters (necrosis, congestion, and inflammation) were evaluated for the pancreas, striated muscle, heart, gallbladder, and urinary bladder damage (the total maximum score is 9).
Buffers
Cortex, Cerebral
Eosin
Ethanol
Fibrosis
Fingers
Formaldehyde
Formalin
Gallbladder
Heart
Hematoxylin
Hemorrhage
Inflammation
Injuries
Kidney
Liver
Lung
Medullas, Kidney
Microscopy
Microtomy
Muscle, Striated
Necrosis
Pancreas
Phosphates
Pulmonary Edema
Quadriceps Femoris
Spleen
Tissues
Transmission Electron Microscopy
Urinary Bladder
Vacuole
Vacuum
Top products related to «Muscle, Striated»
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The M165FC microscope is a high-performance stereo microscope developed by Leica. It features a high-contrast, bright optical system and a flexible stand for a wide range of applications. The M165FC provides continuous magnification from 7.8x to 160x, allowing for detailed observation and inspection of specimens.
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Collagenase type II is a purified enzyme derived from Clostridium histolyticum. It is used for the dissociation of a variety of cell types, particularly those with a high collagen content, such as cartilage and connective tissue.
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More about "Muscle, Striated"
Skeletal muscle, cardiac muscle, sarcomeres, contractile units, exercise physiology, neuromuscular disorders, regenerative medicine, Rompun (xylazine), Trypsin, M165FC microscope, Collagenase type II, TRIzol, Bisbenzimide, 5-bromodeoxyuridine (BrdU), TGF-β1.
Striated muscle is a specialized type of muscle tissue characterized by its distinctive banded appearance under a microscope.
These muscle fibers are composed of repeating contractile units called sarcomeres, which allow for rapid and coordinated movement.
Striated muscle is found in the skeletal muscles that attach to bones and facilitate locomotion, as well as in the cardiac muscle of the heart.
Understanding the structure and function of striated muscle is crucial for research in areas such as exercise physiology, neuromuscular disorders, and regenerative medicine.
Rompun (xylazine) is a sedative and muscle relaxant that may be used in animal studies involving striated muscle.
Trypsin is an enzyme used to dissociate muscle cells, while Collagenase type II is used to break down the extracellular matrix.
TRIzol is a reagent commonly used for RNA extraction from muscle tissue.
Bisbenzimide is a fluorescent dye that can be used to label nuclei, and 5-bromodeoxyuridine (BrdU) is a thymidine analog incorporated into dividing cells.
TGF-β1 is a growth factor that plays a role in muscle regeneration.
Optimize your research on striated muscle with the power of PubCompare.ai's AI-driven platform, which can help you discover the best protocols and products from literature, pre-prints, and patents through intelligent comparisons.
Empowher yourself to make informed decisions and accelerate your discoveries in this important field of study.
Striated muscle is a specialized type of muscle tissue characterized by its distinctive banded appearance under a microscope.
These muscle fibers are composed of repeating contractile units called sarcomeres, which allow for rapid and coordinated movement.
Striated muscle is found in the skeletal muscles that attach to bones and facilitate locomotion, as well as in the cardiac muscle of the heart.
Understanding the structure and function of striated muscle is crucial for research in areas such as exercise physiology, neuromuscular disorders, and regenerative medicine.
Rompun (xylazine) is a sedative and muscle relaxant that may be used in animal studies involving striated muscle.
Trypsin is an enzyme used to dissociate muscle cells, while Collagenase type II is used to break down the extracellular matrix.
TRIzol is a reagent commonly used for RNA extraction from muscle tissue.
Bisbenzimide is a fluorescent dye that can be used to label nuclei, and 5-bromodeoxyuridine (BrdU) is a thymidine analog incorporated into dividing cells.
TGF-β1 is a growth factor that plays a role in muscle regeneration.
Optimize your research on striated muscle with the power of PubCompare.ai's AI-driven platform, which can help you discover the best protocols and products from literature, pre-prints, and patents through intelligent comparisons.
Empowher yourself to make informed decisions and accelerate your discoveries in this important field of study.