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> Chemicals & Drugs > Amino Acid > Dystrophin

Dystrophin

Dystrophin is a large, essential protein found in muscle cells that plays a crucial role in maintaining the structural integrity of muscle fibers.
It acts as a crucial link between the cell's cytoskeleton and the extracellular matrix, providing stability and support.
Disruption or absence of dystrophin can lead to devastating muscular dystrophies, such as Duchenne muscular dystrophy, a debilitating genetic disorder that primarily affects young boys.
Understanding the structure, function, and regulation of dystrophin is crucial for developing effective therapies and improving the lives of individuals affected by these devastating muscle disorders.
PubCompare.ai's powerful tool can optimize Dystrophin research by enhancing reproducibiltiy and accuacy, helping researchers locate the best protocols and products from literature, pre-prints, and patents to improve their Dystrophin-related studies.

Most cited protocols related to «Dystrophin»

1
Assessing Donor-Derived Muscle Fibers
Cited 10 times
Engrafted muscles were removed 4 weeks after cell injection, and when notexin was used, 1 week after myotoxin injection. Muscles that had been grafted with 3F-nLacZ-2E satellite cells were frozen in isopentane cooled in liquid nitrogen. Seven-micrometer transverse cryosections were collected at 100-μm intervals from the entire muscle. Sections were X-gal stained as previously described [27 (link)] and, only if positive signal was detected (thus under-reporting the amount of donor muscle, but avoiding inclusion of host, revertant fibers in our quantification of donor-derived muscle fibers), serial sections were immunostained using primary antibodies rabbit anti-dystrophin (P7) and, in some experiments, with mouse anti-neonatal myosin (BF34; Developmental Studies Hybridoma Bank) after blocking with 10% goat serum.
Collagen VI (Abcam, Cambridge, U.K., http://www.abcam.com) and laminin (Sigma) antibodies were used in representative sections of TA muscle from 3-week-old (n = 4) and 9-month-old (n = 3) mdx-nude mice and of 12- (n = 3) and 24-month-old (n = 2) mdx mice for detection of increase in connective tissue indicative of fibrosis Secondary antibodies used were as follows: Alexa Fluor 488-conjugated goat anti-mouse Ig (Molecular Probes) and Alexa Fluor 594-conjugated goat anti-rabbit Ig (Molecular Probes).
Muscles that had been grafted with Myf5nLacZ/+ satellite cells were fixed in paraformaldehyde and X-gal stained as described elsewhere [3 (link), 27 (link)].
Boldrin L., Zammit P.S., Muntoni F, & Morgan J.E. (2009). Mature Adult Dystrophic Mouse Muscle Environment Does Not Impede Efficient Engrafted Satellite Cell Regeneration and Self-Renewal. Stem cells (Dayton, Ohio), 27(10), 10.1002/stem.162.
Publication 2009
5-bromo-4-chloro-3-indolyl beta-galactoside Alexa594 alexa fluor 488 Antibodies Cells Collagen Connective Tissue Cryoultramicrotomy Dystrophin Fibrosis Freezing Goat Hybridomas Infant, Newborn isopentane Laminin Mice, Inbred mdx Mice, Nude Molecular Probes Mus Muscle Tissue Myosin ATPase myotoxin A Nitrogen notexin paraform Rabbits Serum Tissue Donors
2
Muscle Fiber Typing with Immunofluorescence
Cited 7 times
Serial sections from soleus and plantaris samples were cut at 10 μm using a cryotome (HM 525 Cryostat; Thermo Fisher Scientific, Waltham, MA). Sections were dried at room temperature for 30 min and incubated in a phosphate-buffered saline (PBS) solution containing 0.5% Triton X-100. Sections were rinsed in PBS and subsequently exposed to primary antibodies specific to dystrophin protein (rabbit host, # RB9024R7; Lab Vision Corporation, Fremont, CA), myosin heavy chain Type I (mouse host, immunoglobulin M [IgM] isotype, # A4.840; Developmental Studies Hybridoma Bank, Iowa City, IA), and myosin heavy chain Type IIa (mouse host, immunoglobulin G [IgG] isotype, # SC71; Developmental Studies Hybridoma Bank) in a dark humid chamber at room temperature for 1 h. Sections were subsequently rinsed three times in PBS and exposed to rhodamine red anti-rabbit secondary antibody (R6394; Molecular Probes, Eugene, OR), Alexa Fluor 350 goat anti-mouse IgM isotype-specific secondary antibody (# A31552; Molecular Probes), and Alexa Fluro 488 goat anti-mouse IgG isotype-specific secondary antibody (A11011; Molecular Probes) diluted in PBS containing 0.5% Pierce Super Blocker (Thermo Fisher Scientific) in a dark humid chamber at room temperature for 1 h. Sections were washed in PBS and viewed via a fluorescence microscope (Nikon Instruments, Melville, NY). Fiber typing utilizing this method allows for the individual visualization of the myofiber membrane protein dystrophin using the rhodamine filter set (red), Type I myosin using the DAPI (4′,6-diamidino-2-phenylindole) filter set (blue), Type IIa myosin using the FITC (fluorescein isothiocyanate) filter set (green), and Type IIb/IIx fibers (nonstained/black) myofibers. Images were obtained at a 10× magnification, were merged using NIS-Elements software (Nikon Instruments), and myofibers were analyzed for percent of each MHC by a blinded investigator.
Hyatt H.W., Toedebusch R.G., Ruegsegger G., Mobley C.B., Fox C.D., McGinnis G.R., Quindry J.C., Booth F.W., Roberts M.D, & Kavazis A.N. (2015). Comparative adaptations in oxidative and glycolytic muscle fibers in a low voluntary wheel running rat model performing three levels of physical activity. Physiological Reports, 3(11), e12619.
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Publication 2015
Alexa 350 Antibodies Antibodies, Anti-Idiotypic DAPI Dystrophin Fibrosis Fluorescein Fluorescein-5-isothiocyanate Goat Hybridomas Immunoglobulin G Immunoglobulin Isotypes Immunoglobulin M Isothiocyanates Membrane Proteins Microscopy, Fluorescence Molecular Probes Mus Myosin ATPase Myosin Heavy Chains Myosin Type I Nonmuscle Myosin Type IIA Phosphates Plantaris Muscle Proteins Rabbits Rhodamine Saline Solution Soleus Muscle Triton X-100 Vision
3
Antibody Characterization of Dystroglycan and Sarcoglycan
Cited 7 times
Monoclonal antibodies IIH6 against α-dystroglycan (Ervasti and Campbell, 1991 (link)) and 8D5 against β-dystroglycan (Lim et al., 1995 (link)) were previously characterized. mAbs 20A6 against α-sarcoglycan, 5B1 against β-sarcoglycan, and 21B5 against γ-sarcoglycan were generated in collaboration with L.V.B. Anderson (Newcastle General Hospital, Newcastle upon Tyne, UK). We used a mAb against caveolin-3 (Transduction Laboratories, Lexington, KY). Rabbit polyclonal antibodies against α-sarcoglycan (Roberds et al., 1993a), dystrophin, and utrophin (Ohlendieck et al., 1991a), neuronal nitric oxide synthase (Crosbie et al., 1998 (link)), the α1 subunit of the dihyrdopyridine receptor (Ohlendieck et al., 1991b), and the laminin α2-chain (Allamand et al., 1997 (link)) were described previously. Two affinity-purified rabbit antibodies (rabbit 208 and 215) were produced against a full-length COOH-terminal fusion protein of γ-sarcoglycan, and against an NH2-terminal peptide (MMPQEQYTHHRSTMPGAA) of δ-sarcoglycan, respectively. An affinity-purified goat antibody (goat 26) was produced against a NH2-terminal fusion protein of β-sarcoglycan containing amino acids 1–65. Polyclonal antibodies against α-dystroglycan fusion protein D were affinity-purified from goat 20 (Ibraghimov-Beskrovnaya et al., 1992 (link)). An affinity-purified rabbit antibody (rabbit 235) was produced against a COOH-terminal fusion protein of sarcospan (CFVMWKHRYQVFYVGVGLRSLMASDGQLPKA). Two polyclonal antibodies against ε-sarcoglycan were used. One was previously characterized (Ettinger et al., 1997 (link)) and the other (rabbit 232) was generated against a COOH-terminal peptide of ε-sarcoglycan (PHQTQIPQQQTTGKWYP).
Duclos F., Straub V., Moore S.A., Venzke D.P., Hrstka R.F., Crosbie R.H., Durbeej M., Lebakken C.S., Ettinger A.J., van der Meulen J., Holt K.H., Lim L.E., Sanes J.R., Davidson B.L., Faulkner J.A., Williamson R, & Campbell K.P. (1998). Progressive Muscular Dystrophy in α-Sarcoglycan–deficient Mice. The Journal of Cell Biology, 142(6), 1461-1471.
Publication 1998
alpha-Dystroglycan Amino Acids Antibodies Caveolin 3 Dystroglycans Dystrophin epsilon-Sarcoglycan Goat Immunoglobulins Laminin NOS1 protein, human Peptides Proteins Protein Subunits Rabbits Sarcoglycans SSPN protein, human Staphylococcal Protein A Utrophin
4
Retinal Immunohistochemistry and Imaging
Cited 5 times
Mice were anesthetized with Nembutal and either enucleated directly or perfused with phosphate-buffered saline (PBS) followed by 4% paraformaldehyde (wt/vol) in PBS. Eyes were collected and fixed for 30 min in paraformaldehyde on ice and then rinsed with PBS. Cryosections and whole-mount retinas were prepared as described5 (link). Briefly, sections were incubated in blocking solution (3% normal donkey serum and 0.3% Triton X-100 (vol/vol) in PBS), followed by incubation with primary and secondary antibodies (Invitrogen or Jackson ImmunoResearch). Following washing, sections were mounted in Vectashield (Vectorlabs). Retinas from 3–9 mice were analyzed in each experimental group.
The primary antibodies in this study recognized the following molecules: calbindin (1:2,500, CB38a, Swant), GFP (1:1,000, AB16901, Chemicon), protein kinase Cα (PKCα, 1:500, ab31, AbCam), potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4 (HCN4, 1:500, 75–150, Neuromabs), calsenilin (KChip, 1:100, 75-005, Neuromabs), cre (1:500, MMS-106P, Covance), mouse cone arrestin (mCAR, 1:1,000, provided by C. Craft, University of Southern California56 (link)), recoverin (1:4,000, AB5585, Millipore), protein kinase A, regulatory subunit IIβ (PKARIIb, 1:1,500, 610625, BD Biosciences), PSD-95 (1:200, MA1-046, Thermo Scientific), RIBEYE (1:500, 192 003, Synaptic Systems), Bassoon (1:500, VAM-PS003, Enzo Life Sciences), Piccolo (1:500, 142 003, Synaptic Systems), dystrophin (1:20, NCL-DYS2, Novacastra), and dihydropyridine-sensitive calcium channel α1 subunit (CACNA1, 1:2,000, MAB427, Millipore. TO-PRO-3 (Invitrogen) was used to visualize nuclei. Images were acquired on an Olympus FluoView FV1000 confocal microscope and processed using ImageJ.
Samuel M.A., Voinescu P.E., Lilley B.N., de Cabo R., Foretz M., Viollet B., Pawlyk B., Sandberg M.A., Vavvas D.G, & Sanes J.R. (2014). LKB1 and AMPK regulate synaptic remodeling in old age. Nature neuroscience, 17(9), 1190-1197.
Publication 2014
Antibodies Arrestin Calbindins Calcium Channel Cancer-Associated Retinopathy Antigen Cell Nucleus Cryoultramicrotomy Cyclic AMP-Dependent Protein Kinases Cyclic Nucleotide-Gated Cation Channels dihydropyridine Dystrophin Equus asinus Eye Kv Channel-Interacting Protein 3 Microscopy, Confocal Mus Nembutal paraform Phosphates Potassium PRKCA protein, human Protein Kinase C alpha Protein Subunits Retina Retinal Cone Saline Solution Serum Sodium Triton X-100
5
Systemic-intraosseous Delivery of Dystrophin-expressing Chimeric Cells to mdx Mice
Cited 4 times
Dystrophin Expressing Chimeric cells were prepared for systemic-intraosseous injections to the femoral bone of the mdx mice as previously reported [43 (link), 45 (link), 46 (link)]. Briefly, DEC were counted and washed in sterile saline and viability was assessed with 0.4% Trypan Blue. A single DEC dose was suspended in 60 μl of total volume of saline and transferred to tuberculin syringe with 27G needle (ThermoFischer, Waltham, MA, USA). Mdx recipients were anesthetized with 1.5% isoflurane inhalation and injected with subcutaneous buprenorphine SR lab (0.1 mg/kg) for analgesia. Following a 5-mm skin incision over the mid-femoral level, the subcutaneous tissue and the overlying muscles were dissected. The opening was made in the femoral bone with 28G needle passing through the cortex into the medullary cavity of the femur and 60 μl of the recipient bone marrow were aspirated prior to DEC injection. Next, DEC cells and controls were suspended in 60 μl of sterile saline solution and were injected into the femoral bone marrow cavity in the respective experimental groups. After injection, the bone was sealed with bone wax to prevent cell leakage. The muscle and skin were closed using 4–0 monofilament absorbable suture. Animals were allowed to recover in a heated environment and promptly returned to the colony.
After age-matching the recipient mdx mice were randomized into the following experimental groups: vehicle control (n = 3, 60 μl saline), not-fused MBwt and MBmdx (n = 3, 0.25 × 106/donor–total 0.5 × 106 in 60 μl saline), fused MBwt/MBmdxDEC (n = 4, 0.5 × 106 in 60 μl saline), not-fused MBwt and MSCmdx (n = 3 0.25 × 106 /donor–total 0.5 × 106 in 60 μl saline), and fused MBwt/MSCmdx DEC (n = 3, 0.5 × 106 in 60 μl saline). Animal follow-up consisted of in vivo assessments of echocardiography at day 0 before DEC injection and at 30 and 90 days post-DEC transplant. At day 90 endpoint the animals were euthanized and heart muscles were harvested for histological and immunofluorescence analysis.
Siemionow M., Malik M., Langa P., Cwykiel J., Brodowska S, & Heydemann A. (2019). Cardiac Protection after Systemic Transplant of Dystrophin Expressing Chimeric (DEC) Cells to the mdx Mouse Model of Duchenne Muscular Dystrophy. Stem Cell Reviews and Reports, 15(6), 827-841.
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Publication 2019
Animals Bone Marrow Bones Buprenorphine Cells Chimera Cortex, Cerebral Dental Caries Dystrophin Echocardiography Femur Grafts Immunofluorescence Inhalation Isoflurane Management, Pain Medulla Oblongata Mice, Inbred mdx Muscle Tissue Myocardium Needles Saline Solution Skin Sterility, Reproductive Subcutaneous Tissue Sutures Syringes Tissue Donors Trypan Blue Tuberculin

Most recents protocols related to «Dystrophin»

1
Quantitative Analysis of Dystrophin and Utrophin

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Publication 2023
Biological Assay Dystrophin Goat Heart Hybridomas Immunoglobulins Mice, Inbred C57BL Monoclonal Antibodies Mus Nitrocellulose ponceau S Proteins SDS-PAGE Tissues UTRN protein, human Utrophin
2
Immunoprecipitation of RAB3C and Dystrophin
We incubated the whole‐cell lysates (2 mg) from the cultured cells overnight in IP buffer with 25 μL of protein A/G magnetic beads and the corresponding antibodies against RAB3C (Cat # 15029‐1‐AP, Proteintech, Rosemont, IL, USA) or dystrophin (Cat # HPA023885, Atlas antibodies, Bromma, Sweden) in a 1.5‐mL microcentrifuge tube with a final volume of 1000 μL. We purified the proteins that interacted with the antibodies according to the manufacturer's protocol [38 (link)].
Chang Y., Li C., Chan M., Fang C., Zhang Z., Chen C, & Hsiao M. (2023). Overexpression of synaptic vesicle protein Rab GTPase 3C promotes vesicular exocytosis and drug resistance in colorectal cancer cells. Molecular Oncology, 17(3), 422-444.
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Publication 2023
Antibodies Buffers Cells Cultured Cells Dystrophin G-substrate GIT1 protein, human GTP-Binding Proteins Proteins Staphylococcal Protein A
3
IHC Scoring for RAB3C/Dystrophin Expression in CRC
We devised a four‐point staining‐intensity scoring system to determine the RAB3C/dystrophin expression in the CRC TMA specimens, and the staining intensity scores ranged from 0 (no expression) to 3 (high expression). We classified the results into two groups according to the intensity and extent of the staining: in the low‐expression group; either no staining was present (staining intensity score = 0), or we detected positive staining in fewer than 10% of the cells (staining intensity score = 1); in the high‐expression group, positive immunostaining was present in 10–30% of the cells (staining intensity score = 2), or in more than 30% (staining intensity score = 3). The extent of staining was scored by the percentage of positive cells (0–100%). The final IHC scores (0–300) were obtained by staining intensity score multiplied by the percentage of positive cells. All cases were divided into two groups according to the final IHC scores and processed 50% cutoff. Low IHC expression level was defined as a score less than 150 and a score more than 150 included and 150 itself was defined as high expression. Two pathologists reviewed and independently scored the IHC staining results [30 (link)]. The detailed process and classification are introduced in our previous articles [22 (link)].
Chang Y., Li C., Chan M., Fang C., Zhang Z., Chen C, & Hsiao M. (2023). Overexpression of synaptic vesicle protein Rab GTPase 3C promotes vesicular exocytosis and drug resistance in colorectal cancer cells. Molecular Oncology, 17(3), 422-444.
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Publication 2023
Cells Dystrophin Pathologists
4
Colorectal Adenocarcinoma Tissue Analysis
In total, 215 patients diagnosed with colorectal adenocarcinoma at the Taipei Municipal Wan Fang Hospital of Taiwan from 1998 to 2005 were included in this study. We retrieved the CRC tissues from the Department of Pathology, Taipei Municipal Wan Fang Hospital (Taipei, Taiwan), with Institutional Review Board approval. All experiments were approved by the Ethical Committee (Taipei Medical University‐Joint IRB, approval number: TMU‐IRB 99049). All methodologies conformed to the standards set by the Declaration of Helsinki. Informed consent was signed by all patients and all experiments were approved by the Ethical Committee. We fixed the surgical specimens in 10% buffered neutral formalin and embedded them in paraffin. We reviewed the histological diagnoses, tumor sizes, levels of tumor invasiveness, and lymph node statuses of all the cases, and two pathologists (M.H. and C.L.C.) confirmed them. We determined the final disease stages according to the Cancer Staging System of the American Joint Committee of Cancer (AJCC). We retrospectively collected the clinical data, including data on the follow‐up period, overall survival period, and disease‐free survival period, from each patient's medical record. We followed the patients for more than 152 months or until their deaths. We excluded the patients who died of postoperative complications within 30 days of the surgery from the survival analysis [29 (link)].
We used a tissue microarray (TMA) for the immunohistochemistry (IHC) analysis of the RAB3C expression in this study [22 (link)]. We prepared the TMA containing the CRC tissues and corresponding adjacent noncancerous colon tissues, as previously described [22 (link)]. For each case, we selected three 1‐mm cores from different areas of the tumor tissue. In addition, if available, we also selected two 1‐mm cores of adjacent noncancerous normal colon mucosa for each case. In total, we assembled 243 archival CRC samples for the TMA. The antibodies that we used for the IHC staining included antihuman RAB3C (1:100; Cat # 15029‐1‐AP, Proteintech, Rosemont, IL, USA) and dystrophin (1:50; Cat # HPA023885, Atlas Antibodies, Bromma, Sweden). We performed the immunodetection with an EnVision dual‐link‐system horseradish peroxidase (HRP) detection kit (DAKO, Glostrup, Denmark). The detailed process and classification were introduced in our previous articles [22 (link)].
Chang Y., Li C., Chan M., Fang C., Zhang Z., Chen C, & Hsiao M. (2023). Overexpression of synaptic vesicle protein Rab GTPase 3C promotes vesicular exocytosis and drug resistance in colorectal cancer cells. Molecular Oncology, 17(3), 422-444.
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Publication 2023
Adenocarcinoma Antibodies Arthropathy Colon Diagnosis Dystrophin Formalin GIT1 protein, human Horseradish Peroxidase Joints Malignant Neoplasms Microarray Analysis Mucous Membrane Neoplasm Invasiveness Neoplasms Nodes, Lymph Operative Surgical Procedures Paraffin Pathologists Patients Postoperative Complications Tissue Microarray Analysis Tissues
5
Immunofluorescence Analysis of Muscle Cells
Cultured MPC-myotubes or muscle cryosections (8 μm thickness) were collected for hematoxylin and eosin (H&E) or immunostaining. To perform immunofluorescence assays, cold acetone was first used to fix the samples, followed by incubation with primary antibodies overnight at 4 °C. Antibodies used included rat anti-mouse F4/80 (1:250, eBioscience, 56-4801-80), rabbit anti-mouse IRE1α (p Ser724) (1:250, NOVUS, NB100-2323), mouse anti-mouse eIF2α (p S51) (1:250, Abcam, ab32157), mouse anti-mouse ATF6 (1:250, NOVUS, NBP1-40256), rat anti-mouse CD11b (1:250, eBioscience, 50-0112-82), rabbit anti-mouse dystrophin (1:500, Bioss, bs-14477R), rat anti-mouse laminin (1:200, Abcam, ab11576), rabbit polyclonal anti-fast myosin muscle heavy chain (MyHC, 1:500, abcam, ab91506), rabbit anti-mouse myogenin (1:500, Invitrogen, PA5-116750), rabbit anti-mouse desmin (1:500, abcam, ab32362), rabbit polyclonal anti-myosin-3 (1:500, bs-10905R, bioss), and mouse anti-mouse p38 (1:500, Santa Cruz, sc-166182). The next day, the samples were incubated with goat anti-rat IgG H&L (FITC) (1:500, Abcam, ab6840), Cy3 conjugated goat anti-rat IgG, Cy3 conjugated goat anti-rabbit IgG, Alexa Fluor 488 conjugates goat anti-mouse IgG, or Alexa Fluor 488 conjugates goat anti-rabbit IgG (1:500, Beyotime, A0507, A0516, A0428, A0423). Finally, DAPI was used for counterstaining cell nuclei. An Olympus BX51 fluorescence microscope (Olympus, Japan) was used to analyze the muscle sections or cultured MPCs. For measuring the area ratio of the target protein, more than six images were randomly selected, then the total area of positive protein in the full field of each image and the total area of each image were measured using Image-Pro Plus software (IPP, Media Cybernetics, USA). The area ratio of positive protein [(the total positive area/the total area of each image) × 100%] was calculated. For measuring the intensity of fluorescent staining, the full-image integrated optical density (IOD) and the area of interest (AOI) of all the positive stains were measured in more than six randomly selected images using IPP software. The mean fluorescence staining intensity [(IOD/AOI) × 100%] was then calculated. For measurement of the myofiber cross-sectional area (CSA), 11 randomly selected images were used. First, the total 25–50 fibers area per image (total area, pixels2) were manually evaluated and calculated by image J software (NIH, USA), then the mean myofiber CSA was calculated as the total area/fiber number.
Xiao J., Huang J., Jian X., Wang H., Lan H., Liao Z., Gu R., Hu J, & Liao H. (2023). IRE1α arm of unfolded protein response in muscle-specific TGF-β signaling-mediated regulation of muscle cell immunological properties. Cellular & Molecular Biology Letters, 28, 15.
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Publication 2023
Acetone activating transcription factor 6, human alexa fluor 488 anti-IgG Antibodies Cell Nucleus Cold Temperature Cryoultramicrotomy DAPI Desmin Dystrophin Eosin ERN1 protein, human Fibrosis Fluorescein-5-isothiocyanate Fluorescence Fluorescent Antibody Technique, Direct Goat Hematoxylin ITGAM protein, human Laminin Mesenchymal Stem Cells Mice, House Microscopy, Fluorescence Muscle Tissue Myogenin Myosin ATPase Myosin Heavy Chains Novus Proteins Protein Targeting, Cellular Rabbits Skeletal Myocytes

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1
Ab15277 by Abcam
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Odyssey imaging system by LI COR
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The Odyssey Imaging System is a fluorescence-based imager designed for detection and quantification of proteins and nucleic acids. It utilizes two near-infrared fluorescent dyes to enable multiplex detection and analysis. The system can be used for a variety of applications, including Western blotting, gel and membrane-based assays, and microplate-based assays.
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Pierce bca protein assay kit by Thermo Fisher Scientific
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C57bl 10scsn dmdmdx j by Jackson ImmunoResearch
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C57BL/10ScSn-Dmdmdx/J is a mouse strain that carries a spontaneous mutation in the dystrophin gene, resulting in a model for Duchenne muscular dystrophy. This strain is commonly used in research related to muscular dystrophy and related disorders.
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More about "Dystrophin"

Dystrophin is a crucial structural protein found in muscle cells, acting as a vital link between the cell's internal scaffolding (cytoskeleton) and the surrounding extracellular matrix.
Its primary role is to maintain the integrity and stability of muscle fibers.
Disruption or absence of dystrophin can lead to devastating muscular dystrophies, such as the debilitating Duchenne muscular dystrophy (DMD), which primarily affects young boys.
Understanding the structure, function, and regulation of this large, essential protein is crucial for developing effective therapies and improving the lives of individuals affected by these devastating muscle disorders.
Researchers can optimize their dystrophin-related studies by utilizing powerful tools like PubCompare.ai, which can enhance reproducibility and accuracy by helping them locate the best protocols and products from literature, preprints, and patents.
Key terms and concepts related to dystrophin research include: Ab15277 (a dystrophin-specific antibody), NCL-DYS1 (a dystrophin-specific antibody clone), Odyssey imaging system (for visualizing and quantifying proteins), Pierce BCA Protein Assay Kit (for measuring protein concentration), protease inhibitor cocktail (to protect proteins from degradation), Image Lab 6.1 software (for analyzing protein data), DAPI (a fluorescent dye used to stain nuclei), BCA protein assay kit (another method for determining protein concentration), and the C57BL/10ScSn-Dmdmdx/J mouse model (a common model for studying DMD).
Researchers can also utilize the NuPAGE LDS sample buffer to prepare samples for electrophoresis and Western blotting experiments involving dystrophin.
By incorporating these tools and techniques, scientists can advance their understanding of dystrophin and develop more effective treatments for muscular dystrophies.