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Dystroglycan is a laminin binding component of the dystrophin-glycoprotein complex which provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. Additionally we are shipping Dystroglycan Antibodies (96) and Dystroglycan Proteins (11) and many more products for this protein.
Showing 5 out of 11 products:
Fktn (show FKTN ELISA Kits) deficient mice express moderate to severe muscular dystrophy; glycosylated alpha-dystroglycan has a unique role in muscle regeneration in these mice
5-amino-4-imidazolecarboxamide riboside treatment increases utrophin (show UTRN ELISA Kits) A and beta-dystroglycan expression in mdx (show DMD ELISA Kits) mouse muscle.
Phosphorylation within the cysteine-rich region of dystrophin (show DMD ELISA Kits) enhances its association with beta-dystroglycan and identifies a potential novel therapeutic target for skeletal muscle wasting.
Results suggest that by interfering in the cross-talk between the transmembrane form of the laminin receptor dystroglycan and F-actin, AHNAK1 (show AHNAK ELISA Kits) influences the cytoskeleton organization of Schwann cells
We evaluate the key characteristics of the mdx in comparison with other mouse mutants with inactivations in DAPC components, along with key modifiers of the disease phenotype.
results indicate a novel role for laminin-dystroglycan interactions in the cooperative integration of astrocytes, endothelial cells, and pericytes in regulating the Blood Brain Barrier.
Endogenous glucuronyltransferase activity of LARGE or LARGE2 (show GYLTL1B ELISA Kits) required for functional modification of alpha-dystroglycan in cells and tissues.
Beta-dystroglycan can respond to ezrin (show EZR ELISA Kits) driven cytoskeletal and cell morphology changes,by translocating from the cytoplasm to the nucleus.
Alpha dystroglycan is a perlecan (show HSPG2 ELISA Kits) receptor that specifically functions in the stellate reticulum of the embryonic stage.
The study provides evidence for at least three separate pools of dystroglycan complexes within myofibers that differ in composition and are differentially affected by loss of dystrophin (show DMD ELISA Kits).
Data show that CD93 antigen (show CD93 ELISA Kits) proved to be phosphorylated on tyrosine 628 and 644 following cell adhesion on laminin through dystroglycan.
Novel mutations in DAG1 are associated with asymptomatic hyperCKemia with hypoglycosylation of alpha-dystroglycan.
Depletion of DAG resulted in altered morphology and reduced properties of differentiated HL-60 cells, including chemotaxis, respiratory burst, phagocytic activities and markers of differentiation, implicating DAG as a protein involved in differentiation.
A report of a homozygous novel DAG1 missense mutation c.2006G>T in the beta-subunit (show POLG ELISA Kits) of dystroglycan in two Libyan siblings with with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy.
These data suggest that proteolysis, tyrosine phosphorylation and translocation of dystroglycan to the nucleus resulting in altered gene transcription could be important mechanisms in the progression of prostate cancer.
T192M point-mutation in dystroglycan leads to a weaker interactions with laminin-1 (show LAMA1 ELISA Kits), which leads to hypoglycosylation and which finally leads to the limb girdle disease.
GTDC2 generates CTD110.6 antibody-reactive N-acetylglucosamine epitopes on the O-mannosylated alpha-dystroglycan.
the Dystroglycan-mediated cortical microtubule anchoring, the disruption of which initiates gastrulation EMT (show ITK ELISA Kits).
Results provide evidence that MMP-2 (show MMP2 ELISA Kits) bears the potentiality to cleave alpha-DG enriched from rabbit skeletal muscle indicating that this degradation indeed might also occur in vivo.
Dystroglycan is a laminin binding component of the dystrophin-glycoprotein complex which provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. Dystroglycan 1 is a candidate gene for the site of the mutation in autosomal recessive muscular dystrophies. The dramatic reduction of dystroglycan 1 in Duchenne muscular dystrophy leads to a loss of linkage between the sarcolemma and extracellular matrix, rendering muscle fibers more susceptible to necrosis. Dystroglycan also functions as dual receptor for agrin and laminin-2 in the Schwann cell membrane. The muscle and nonmuscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence. Alternative splicing results in multiple transcript variants all encoding the same protein.
, dystrophin associated glycoprotein 1
, dystrophin-associated glycoprotein 1
, glycine cleavage system T-protein
, RAB7, member RAS oncogene family