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anti-Human Dystrophin Antibodies:
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Fish Monoclonal Dystrophin Primary Antibody for ICC, IF - ABIN267904
Morris, Ellis, Nguyen: A quantitative ELISA for dystrophin. in Journal of immunological methods 1993
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Chicken Monoclonal Dystrophin Primary Antibody for IHC (p), IHC - ABIN267033
Hosur, Kavirayani, Riefler, Carney, Lyons, Gott, Cox, Shultz: Dystrophin and dysferlin double mutant mice: a novel model for rhabdomyosarcoma. in Cancer genetics 2012
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Human Polyclonal Dystrophin Primary Antibody for ICC, IF - ABIN4306551
Aoyama, Kawase, Bando, Monji, Murohara et al.: Dipeptidyl Peptidase 4 Inhibition Alleviates Shortage of Circulating Glucagon-Like Peptide-1 in Heart Failure and Mitigates Myocardial Remodeling and Apoptosis via the Exchange Protein Directly ... in Circulation. Heart failure 2016
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Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.
Forced expression of embryonic dystrophin in zebrafish using an exon-skipping approach severely impairs the mobility and muscle architecture.
Spatio-temporal differences in dystrophin dynamics at mRNA and protein levels have been revealed using a novel reporter system.
Data indicate that ataluren (0.1-1 muM, 3-5 dpf) improved contractile function (~60% improvement of force at 0.5 muM) and dystrophin expression.
early expression of the short carboxyl-terminal dystrophin transcript, with expression of the full length muscle transcript occurring during myogenesis.
Data suggest that dystrophin functions in regulation of calcium signaling during early stages of slow muscle cell differentiation; calcium signaling in these cells coincide with first spontaneous contractions of embryonic trunk.
analysis of the dystrophin associated protein complex in zebrafish
Data suggest that the progressive muscle degeneration phenotype of dystrophin mutant zebrafish embryos is caused by the failure of embryonic muscle end attachments.
Dystrophin family gene expression in zebrafish is reported.
reduction of dystrophin, dystroglycan and sarcoglycan (show SGCD Antibodies) at translational level in embryos with overexpressed myostatin2
Data indicate that skeletal muscles from with a missense mutation in the dystrophin gene is associated with muscle histophatology.
Mutation spectrum analysis of DMD gene causing Duchenne/Becker muscular dystrophy in 68 families in Kuwait has been reported.
Low dystrophin expression is associated with Becker and Duchenne muscular dystrophy.
This study characterize the developmental profile of dystrophin expression across human brain regions to define the temporal profile of astrocytic endfoot development.
A novel small mutation in the first exon-intron boundary splicing site of the DMD gene was found, in a patient with higher serum CK level in his family. This small mutation is responsible for X-linked dilated cardiomyopathy.
new mutations in Duchenne muscular dystrophy/Becker muscular dystrophy patients with deletions were significantly more frequent than in those with duplications and small mutations.
Ambulant and steroid naive Japanese Duchenne muscular dystrophy was shown significantly shorter than normal. In addition, Becker muscular dystrophy was slightly shorter than normal. This suggested that levels of dystrophin expression is associated with short stature. The fact that the higher incidence of the short stature was observed in Dp71 subgroup suggested a role of Dp71 in growth.
Data indicate that Becker muscular dystrophy (BMD (show BEST1 Antibodies)) patients carrying deletions of the rod domain of the exons in dystrophin gene.
It has been concluded that patients with dystrophin "del x-51" or "del 48" mutations have mild or asymptomatic Becker muscular dystrophy, while "del 45-x" mutations cause comparatively severe weakness, and functional deterioration in 1 year.
The study and validation of DMD as a new player in tumor development and as a new prognostic factor for tumor progression and survival are warranted.
The entire DMD locus is dynamically transcribed by the RNA pol II (show 0 Antibodies); mechanisms involved in dystrophin gene expression control.
Influence of full-length dystrophin on brain volumes in mouse models of Duchenne muscular dystrophy
Impaired regenerative capacity and lower revertant fibre expansion in dystrophin-deficient Duchenne muscular dystrophy mouse muscles on DBA (show RPS19 Antibodies)/2 background has been reported.
these results provide new insights into the spatial distribution of dystrophin glycoprotein components and their dynamics in living mice.
it is concluded that the LVH with high LVEDWS is associated to a degradation of dystrophin and increase of myocardial stiffness. At least in a murine model these alterations were attenuated after the administration of a matrix metalloprotease inhibitor.
Dystrophin-glycoprotein complex component dystroglycan 1 (Dag1) directly binds to the Hippo pathway effector Yap to inhibit cardiomyocyte proliferation in mice
CRIPSR-mediated genome editing efficiently excised the mutant exon 23 in dystrophic mice, restoring the expression of dystrophin protein expression in dystrophic cardiac muscles to a level approaching 40% and improving myocardial contraction.
We show that strong and specific expression of exogenous Dp71 in Muller cells leads to correct localization of Dp71 protein restoring all protein interactions in order to re-establish a proper functional BRB (show PTBP1 Antibodies) and retina homeostasis thus preventing retina from oedema.
avoiding vector genome loss after AAV injection by PPMO pre-treatment would allow efficient long-term restoration of dystrophin and the use of lower and thus safer vector doses for Duchenne patients.
To optimize a dystrophin cDNA construct for therapeutic application we designed and produced four human minidystrophins within the packaging capacity of lentiviral vectors. Two novel minidystrophins retained the centrally located neuronal nitric oxide synthase (nNOS (show NOS1 Antibodies))-anchoring domain in order to achieve sarcolemmal nNOS (show NOS1 Antibodies) restoration, which is lost in most internally deleted dystrophin constructs.
Our study demonstrates for the first time that low-level dystrophin can partially preserve heart function.
Dys protein regulates tarsal joint formation in response to Notch (show NOTCH1 Antibodies) activity during Drosophila leg development.
The findings suggest that the signaling functions of Dystrophin protein are able to ameliorate dilated cardiomyopathy, and thus might help to improve heart muscle function in micro-Dystrophin-based gene therapy approaches.
Nrk, mbl, capt and Cam genetically interact with dystrophin and/or dystroglycan in the process of axon path-finding in the eye.
only dystroglycan, but not dystrophin deficiency causes myodegeneration induced by energetic stress suggesting that dystroglycan might be a component of the low-energy pathway and act as a transducer of energetic stress in normal and dystrophic muscles
Dystrophin and the Rho GTPase (show RACGAP1 Antibodies) crossveinless-c signaling pathway likely interact at the postsynaptic side of the NMJ to maintain synaptic homeostasis.
Lack of the large dystrophin isoforms in the postsynaptic muscle cell leads to elevated evoked neurotransmitter release from presynaptic terminals.
Our results indicate the existence of at least two possibly separate roles of dystrophin in muscle, maintaining synaptic homeostasis and preserving the structural stability of the muscle.
The det locus encodes Drosophila dys, which acts with other components of the DAPC to influence intercellular signalling in developing wing veins.
Possibility that Dp186 modulates other non-Gbb/Wit-dependent retrograde signaling pathways required to maintain normal synaptic physiology.
The dystrophin gene is the largest gene found in nature, measuring 2.4 Mb. The gene was identified through a positional cloning approach, targeted at the isolation of the gene responsible for Duchenne (DMD) and Becker (BMD) Muscular Dystrophies. DMD is a recessive, fatal, X-linked disorder occurring at a frequency of about 1 in 3,500 new-born males. BMD is a milder allelic form. In general, DMD patients carry mutations which cause premature translation termination (nonsense or frame shift mutations), while in BMD patients dystrophin is reduced either in molecular weight (derived from in-frame deletions) or in expression level. The dystrophin gene is highly complex, containing at least eight independent, tissue-specific promoters and two polyA-addition sites. Furthermore, dystrophin RNA is differentially spliced, producing a range of different transcripts, encoding a large set of protein isoforms. Dystrophin (as encoded by the Dp427 transcripts) is a large, rod-like cytoskeletal protein which is found at the inner surface of muscle fibers. Dystrophin is part of the dystrophin-glycoprotein complex (DGC), which bridges the inner cytoskeleton (F-actin) and the extra-cellular matrix.
dystrophin (muscular dystrophy, Duchenne and Becker types)
, Duchenne muscular dystrophy
, dystrophin isoform Dp116
, dystrophin Dp71 isoform
, X-linked muscular dystrophy
, dystrophin transcript variant Dp71e
, dystrophin, muscular dystrophy
, Dystrophin-like protein 1
, Dystrophin-like protein 186
, Dystrophin-like protein 2
, Dystrophin-like protein 3
, dystrophin Dp186