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LARGE, which is one of the largest in the human genome, encodes a member of the N-acetylglucosaminyltransferase gene family. Additionally we are shipping Like-Glycosyltransferase Antibodies (44) and Like-Glycosyltransferase Proteins (7) and many more products for this protein.
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This study suggests LARGE as the first known modifier of plasma antithrombin (show SERPINC1 ELISA Kits).
results reveal that the LARGE-glycan of dystroglycan serves as a tunable extracellular matrix protein scaffold, the extension of which is required for normal skeletal muscle function
LARGE could act as a bifunctional glycosyltransferase, with xylosyltransferase and glucuronyltransferase activities, which produced repeating units of [-3-xylose-alpha1,3-glucuronic acid-beta1-]; allowed alpha-DG to bind laminin-G domain-containing ECM (show MMRN1 ELISA Kits) ligands
the ligand-binding activity of alpha-dystroglycan is conferred primarily by LARGE modification at Thr (show TRH ELISA Kits)-317 and -319, within the highly conserved first 18 amino acids of the mucin (show SLC13A2 ELISA Kits)-like domain
LARGE2 was found to support the maturation of alpha-dystroglycan more effectively than LARGE.
LARGE repression is responsible for the defects in dystroglycan-mediated cell adhesion that are observed in epithelium-derived cancer cells and point to a defect of dystroglycan glycosylation as a factor in cancer progression
These findings indicate that the fine-tuning of AMPA (show GRIA3 ELISA Kits)-R trafficking by LARGE at the Golgi is critical for hippocampus-dependent memory in the brain.
data suggest LARGE overexpression may only be deleterious under a forced regenerative context, such as that resulting from a reduction in FKRP (show FKRP ELISA Kits): in the absence of such a defect we show that systemic expression of LARGE can indeed act therapeutically, and that even dramatic LARGE overexpression is well-tolerated in heart and skeletal muscle
MBP1 inhibits Ab fibril formation in vitro and demonstrate the ability of MBP1 to reduce Ab pathology and improve behavioral performance.
The overexpression of LARGE aggravates muscular dystrophy by suppressing the muscle regeneration and this adverse effect is mediated via reduced expression of IGF-1 (show IGF1 ELISA Kits).
Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of alpha-dystroglycan in cells and tissues.
The overexpression of LARGE leads to a shortened lifespan and worsening of the FKRP (show FKRP ELISA Kits)-MD phenotype
blocking Large during muscle regeneration results in synthesis of dystroglycan with minimal LARGE-glycan repeats in association with less compact basement membrane, immature neuromuscular junctions, and dysfunctional muscle predisposed to dystrophy
Muscular dystrophy defects are primarily due to the effects of LARGE and glycosylated dystroglycan in stabilizing the endplate of the neuromuscular junction.
Differential glycosylation of alpha-dystroglycan and proteins other than alpha-dystroglycan by like-glycosyltransferase.
This gene, which is one of the largest in the human genome, encodes a member of the N-acetylglucosaminyltransferase gene family. It encodes a glycosyltransferase which participates in glycosylation of alpha-dystroglycan, and may carry out the synthesis of glycoprotein and glycosphingolipid sugar chains. It may also be involved in the addition of a repeated disaccharide unit. Mutations in this gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan. Alternative splicing of this gene results in two transcript variants that encode the same protein.
, glycosyltransferase-like 1B-B
, glycosyltransferase-like protein LARGE2-B
, acetylglucosaminyltransferase-like 1A
, acetylglucosaminyltransferase-like protein
, glycosyltransferase-like protein LARGE1
, glycosyltransferase-like 1A
, glycosyltransferase-like protein LARGE1-like
, eosinophil granule major basic protein 1
, prepro major basic protein 1