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Treatment with the anti-IL-6 receptor antibody attenuates muscular dystrophy via promoting skeletal muscle regeneration in dystrophin-/utrophin-deficient mice.
Continual will increase within the ranges of the inflammatory cytokine interleukin-6 (IL-6) in serum and skeletal muscle are thought to contribute to the development of muscular dystrophy. Dystrophin/utrophin double-knockout (dKO) mice develop a extra extreme and progressive muscular dystrophy than the mdx mice, the commonest murine mannequin of Duchenne muscular dystrophy (DMD).
Specifically, dKO mice have smaller physique sizes and muscle diameters, and develop progressive kyphosis and fibrosis in skeletal and cardiac muscular tissues. As mdx mice and DMD sufferers, we discovered that IL-6 ranges within the skeletal muscle had been considerably elevated in dKO mice. Thus, on this research, we aimed to research the consequences of IL-6 receptor (IL-6R) blockade on the muscle pathology of dKO mice.
Restoration of pharyngeal dilator muscle pressure in dystrophin-deficient (mdx) mice following co-treatment with neutralizing interleukin-6 receptor antibodies and urocortin 2.
What’s the central query of this research? We beforehand reported impaired higher airway dilator muscle perform within the mdx mouse mannequin of Duchenne muscular dystrophy (DMD). Our purpose was to evaluate the impact of blocking interleukin-6 receptor signalling and stimulating corticotrophin-releasing issue receptor 2 signalling on mdx sternohyoid muscle construction and performance. What’s the principal discovering and its significance?
The interventional remedy had a optimistic inotropic impact on sternohyoid muscle pressure, restoring mechanical work and energy to wild-type values, lowered myofibre central nucleation and preserved the myosin heavy chain sort IIb fibre complement of mdx sternohyoid muscle. These information may need implications for improvement of pharmacotherapies for DMD with relevance to respiratory muscle efficiency.
The mdx mouse mannequin of Duchenne muscular dystrophy exhibits proof of impaired pharyngeal dilator muscle perform. We hypothesized that inflammatory and stress-related elements are implicated in airway dilator muscle dysfunction. Six-week-old mdx (n = 26) and wild-type (WT; n = 26) mice obtained both saline (0.9% w/v) or a co-administration of neutralizing interleukin-6 receptor antibodies (0.2 mg kg-1 ) and corticotrophin-releasing issue receptor 2 agonist over 2 weeks.
Sternohyoid muscle isometric and isotonic contractile perform was examined ex vivo. Muscle fibre centronucleation and muscle mobile infiltration, collagen content material, fibre-type distribution and fibre cross-sectional space had been decided by histology and immunofluorescence.
Muscle chemokine content material was examined by use of a multiplex assay. Sternohyoid peak particular pressure at 100 Hz was considerably lowered in mdx in contrast with WT. Drug remedy fully restored pressure in mdx sternohyoid to WT ranges. The proportion of centrally nucleated muscle fibres was considerably elevated in mdx, and this was partly ameliorated after drug remedy.
The areal density of infiltrates and collagen content material had been considerably elevated in mdx sternohyoid; each indices had been unaffected by drug remedy. The abundance of myosin heavy chain sort IIb fibres was considerably decreased in mdx sternohyoid; drug remedy preserved myosin heavy chain sort IIb complement in mdx muscle.
The chemokines macrophage inflammatory protein 2, interferon-γ-induced protein 10 and macrophage inflammatory protein 3α had been considerably elevated in mdx sternohyoid in contrast with WT. Drug remedy considerably elevated chemokine expression in mdx however not WT sternohyoid.
Restoration of contractile perform was spectacular in our research, with implications for Duchenne muscular dystrophy. The exact molecular mechanisms by which the drug remedy exerts an inotropic impact on mdx sternohyoid muscle stay to be elucidated.
Characterization of 65 epitope-specific dystrophin monoclonal antibodies in canine and murine fashions of duchenne muscular dystrophy by immunostaining and western blot.
Epitope-specific monoclonal antibodies can present distinctive insights for finding out mobile proteins. Dystrophin is without doubt one of the largest cytoskeleton proteins encoded by 79 exons. The absence of dystrophin leads to Duchenne muscular dystrophy (DMD). During the last twenty years, dozens of exon-specific human dystrophin monoclonal antibodies have been developed and efficiently used for DMD analysis.
Sadly, nearly all of these antibodies haven’t been completely characterised in dystrophin-deficient canines, an excellent massive animal mannequin for translational analysis. To fill the hole, we carried out a complete research on 65 dystrophin monoclonal antibodies in regular and dystrophic canines (coronary heart and skeletal muscle) by immunofluorescence staining and western blot.
For comparability, we additionally included striated muscular tissues from regular BL10 and dystrophin-null mdx mice. Our evaluation revealed distinctive species, tissue and assay-dependent recognition patterns of various antibodies.
Importantly, we recognized 15 antibodies that may persistently detect full-length canine dystrophin in each immunostaining and western blot. Our outcomes will function an vital reference for finding out DMD within the canine mannequin.
Profitable histocompatible myoblast transplantation in dystrophin-deficient mdx mouse regardless of the manufacturing of antibodies in opposition to dystrophin.
Myoblast transplantation has been thought-about a possible remedy for some muscular problems. It has confirmed very profitable, nonetheless, solely in immunodeficient or immunosuppressed mice. On this research, myoblasts from C57BL10J +/+ mice had been transplanted, with no immunosuppressive remedy, within the tibialis anterior of absolutely histocompatible however dystrophin-deficient C57BL10J mdx/mdx mice.
One to 9 months after transplantation, the success of the graft was evaluated by immunohistochemistry. All of the transplanted mice developed dystrophin-positive fibers following transplantation. Relying on myoblast cultures, transplantations, and time of study, the mice introduced 15 to 80% of dystrophin-positive fibers in transplanted muscular tissues.
These fibers had been accurately oriented they usually had been both from donor or hybrid origin. The dystrophin-positive fibers remained steady as much as 9 months. Attainable humoral and mobile immune responses had been investigated after grafting. Antibodies directed in opposition to dystrophin and/or muscle membrane had been developed by 58% of the mice as demonstrated by immunohistochemistry and Western blotting.
Regardless of the presence of those antibodies, dystrophin-positive fibers had been nonetheless current in grafted muscular tissues 9 months after transplantation. Furthermore, the muscular tissues didn’t present huge infiltration by CD4 cells, CD8 cells, or macrophages, as already described in myoblast allotransplantations.
This lack of rejection was attributed to the sequestrated nature of dystrophin after fiber formation. These outcomes point out that myoblast transplantation results in fiber formation when immunocompetent however absolutely histocompatible donors and recipients are used and that dystrophin incompatibility alone is just not ample to induce an immunological rejection response.
Specificity and VH sequence of two monoclonal antibodies in opposition to the N-terminus of dystrophin.
Now we have used a random library of 15-mer peptides expressed on phage to point out that two monoclonal antibodies (mAbs) require solely the primary three amino acids of dystrophin (Leu-Trp-Trp) for binding. Because the mAbs acknowledge dystrophin in frozen muscle sections, the outcomes counsel that this hydrophobic N-terminus of dystrophin is accessible to antibody in situ.
Quantitative binding research prompt minor variations in specificity between the 2 mAbs, so the Ig heavy-chain variable area (VH) sequences of the 2 hybridomas had been decided by RT-PCR and cDNA sequencing. After elimination of PCR errors, the 2 cDNA sequences had been discovered to be an identical apart from 5 somatic mutations which resulted in three amino acid modifications within the second hypervariable area (CDR2).
Dystrophin Antibody |
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| ABD8748 | Lifescience Market | 100 ug | EUR 525.6 |
Dystrophin Antibody |
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| R30032 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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Description: Dystrophin(DMD) gene has 79 exons spanning at least 2,300 kb(2.3 Mb). The C terminus of the dystrophin protein is encoded by a highly conserved, alternatively spliced region of the gene. beta-dystroglycan binding activity is expressed by the dystrophin fragment spanning amino acids 3026-3345 containing the ZZ domain. DMD transcript is formed by at least 60 exons; the first half of the transcript is formed by a minimum of 33 exons spanning nearly 1000 kb, and the remaining portion has at least 27 exons that may spread over a similar distance. Dystrophin gene is expressed at a higher level in primary cultures of neuronal cells than in astro-glial cells derived from adult mouse brain. overexpression of dystrophin prevents the development of the abnormal mechanical properties associated with dystrophic muscle without causing deleterious side effects. |
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Dystrophin Antibody |
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| R31689 | NSJ Bioreagents | 100 ug | EUR 356.15 |
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Description: Dystrophin, also known as DMD, is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. It is mapped to Xp21.2-p21.1. This complex is variously known as the costamere or thedystrophin-associated protein complex. Many muscle proteins, such as alpha-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with Dystrophin at the costamere. Dystrophin is a protein located between the sarcolemma and the outermost layer of myofilaments in the muscle fiber (myofiber). It is a cohesive protein, linking actin filaments to another support protein that resides on the inside surface of each muscle fiber’s plasma membrane (sarcolemma). |
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Dystrophin Antibody |
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| DF8748 | Affinity Biosciences | 100ul | EUR 280 |
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Description: Human,Mouse,Rat |
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Dystrophin Antibody |
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| DF8748-100ul | Affinity Biosciences | 100ul | EUR 280 |
Dystrophin Antibody |
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| DF8748-200ul | Affinity Biosciences | 200ul | EUR 350 |
Dystrophin Antibody |
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| E19-8748-1 | EnoGene | 50ug/50ul | EUR 145 |
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Description: Available in various conjugation types. |
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Dystrophin Antibody |
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| E19-8748-2 | EnoGene | 100ug/100ul | EUR 225 |
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Description: Available in various conjugation types. |
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Dystrophin Antibody / DMD |
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| V8862-100UG | NSJ Bioreagents | 100ug | EUR 349.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V8862-20UG | NSJ Bioreagents | 20ug | EUR 153.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V8862SAF-100UG | NSJ Bioreagents | 100ug | EUR 349.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V4009-100UG | NSJ Bioreagents | 100 ug | EUR 349.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V4009-20UG | NSJ Bioreagents | 20 ug | EUR 153.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V4009SAF-100UG | NSJ Bioreagents | 100 ug | EUR 349.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| RQ5369 | NSJ Bioreagents | 100 ul | EUR 356.15 |
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Description: The DMD gene spans a genomic range of greater than 2 Mb and encodes a large protein containing an N-terminal actin-binding domain and multiple spectrin repeats. The encoded protein forms a component of the dystrophin-glycoprotein complex (DGC), which bridges the inner cytoskeleton and the extracellular matrix. Deletions, duplications, and point mutations at this gene locus may cause Duchenne muscular dystrophy (DMD), Becker muscular dystrophy (BMD), or cardiomyopathy. Alternative promoter usage and alternative splicing result in numerous distinct transcript variants and protein isoforms for this gene. [RefSeq] |
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Dystrophin Antibody / DMD |
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| V7540-100UG | NSJ Bioreagents | 100 ug | EUR 349.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V7540-20UG | NSJ Bioreagents | 20 ug | EUR 153.3 |
|
Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V7540IHC-7ML | NSJ Bioreagents | 7 ml | EUR 349.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V7540SAF-100UG | NSJ Bioreagents | 100 ug | EUR 349.3 |
|
Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
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| V7547-100UG | NSJ Bioreagents | 100 ug | EUR 349.3 |
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Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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Dystrophin Antibody / DMD |
|||
| V7547-20UG | NSJ Bioreagents | 20 ug | EUR 153.3 |
|
Description: Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least 8 independent tissue-specific promoters and 2 poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission. |
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The outcomes counsel that the 2 hybridomas originated from the identical lymphocyte clone in a germinal centre of the spleen, however underwent completely different level mutations and subtype switches throughout clonal growth to kind blast cells.
