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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. Zusätzlich bieten wir Ihnen Diacylglycerol Antikörper (4) und und viele weitere Produktgruppen zu diesem Protein an.
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All Species DAG ELISA Kit für Competition ELISA - ABIN4947513
Lu, Zhang, Zhang, Li, Wang, Xu, Liu, Li, Dong, Zhang: Pigment Epithelium-Derived Factor (PEDF) Improves Ischemic Cardiac Functional Reserve Through Decreasing Hypoxic Cardiomyocyte Contractility Through PEDF Receptor (PEDF-R). in Journal of the American Heart Association 2016
N-terminal alpha Dystroglycan ELISA signals were significantly reduced in Duchenne muscular dystrophy (zeige DMD ELISA Kits) serum relative to serum from otherwise normal controls.
TMEM5 is a UDP-xylosyl transferase that elaborates the O-mannose glycan structure on alpha-dystroglycan. The authors demonstrate in a zebrafish model as well as in a human patient that defects in TMEM5 result in muscular dystrophy in combination with abnormal brain development.
Our results strongly suggest that the balance and integrity between the dystroglycan alpha and beta subunits are indispensable and responsible for the cell differentiation and proliferation in acute leukemia cells.
interation of DG with laminin and dynamin (zeige DNM1 ELISA Kits) is involved in the regulation of AQP4 (zeige AQP4 ELISA Kits) internalization
The Muscular Dystrophy Gene TMEM5 Encodes a Ribitol beta1,4-Xylosyltransferase Required for the Functional Glycosylation of Dystroglycan.
Data show that CD93 antigen proved to be phosphorylated on tyrosine 628 and 644 following cell adhesion on laminin through dystroglycan.
Phosphorylation within the cysteine-rich region of dystrophin (zeige DMD ELISA Kits) enhances its association with beta-dystroglycan and identifies a potential novel therapeutic target for skeletal muscle wasting.
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 of dystroglycan in two Libyan siblings with with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy.
we review the human and mouse Ly6/uPAR (zeige PLAUR ELISA Kits) family gene and protein structure and genomic organization, expression, functions, and evolution, and introduce new names for novel family members
Data suggest that expression of Ly6 in mouse placenta is restricted to differentiated syncytiotrophoblast; Ly6 may be a biomarker for syncytiotrophoblast progenitor cells.
Ly6C-expressing inflammatory monocytes are the early and dominant infiltrating cells in the central nervous system during experimental autoimmune encephalomyelitis, a model for the acute phase of multiple sclerosis.
The myeloid 7/4-antigen defines recently generated inflammatory macrophages and is synonymous with Ly-6B.
Strong evidence is provided that susceptibility to mouse adenovirus type 1 (MAV-1) is encoded by one or more members of the Ly6 gene complex.
CD73 and Ly-6A/E (zeige Ly6a ELISA Kits) expression identify a population of Th primed precursor-like cells in C57BL/6 mice and at least some other Ly-6.2 mice.
Atherogenic lesion size highly correlates with the number of circulating bone marrow monocytes, particularly the Ly6G-negative 7/4(lo) monocyte subset.
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.