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The protein encoded by POMT1 is an O-mannosyltransferase that requires interaction with the product of the POMT2 gene for enzymatic function. Additionally we are shipping Protein-O-Mannosyltransferase 1 Kits (4) and Protein-O-Mannosyltransferase 1 Proteins (4) and many more products for this protein.
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Human Polyclonal POMT1 Primary Antibody for EIA, FACS - ABIN954244
Manya, Akasaka-Manya, Nakajima, Kawakita, Endo: Role of N-glycans in maintaining the activity of protein O-mannosyltransferases POMT1 and POMT2. in Journal of biochemistry 2010
Show all 2 references for ABIN954244
Inhibition of POMT1/2 in human mesencyhmal stem cells , resulted in complete abolishment of chondrogenesis and alterations of adipogenic and osteogenic potential together with a lethal effect during myogenic induction.
Three patients with heterozygous POMT1 mutations showed left ventricular (LV) dilation and/or decrease in myocardial contractile force.
the effects of replacing Arg(64), Glu (show DCTN1 Antibodies)(78) and Arg(138)residues in human POMT1 and POMT2 (show POMT2 Antibodies) with Ala on complex formation and enzymatic activity were studied.
the function of the gene products is only known for POMT1, POMT2 (show POMT2 Antibodies), and POMGnT1 (show POMGNT1 Antibodies), all responsible for the O-mannosylglycan biosynthesis
the N-glycosylation of POMT1 and POMT2 (show POMT2 Antibodies) is required for maintaining the conformation as well as the activity of the POMT1-POMT2 (show POMT2 Antibodies) complex.
Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome
Extracellular matrix and nuclear abnormalities in skeletal muscle of a patient with Walker-Warburg syndrome caused by POMT1 mutation.
active enzyme complex of POMT1 and POMT2 (show POMT2 Antibodies) suggests that the regulation of protein O-mannosylation is complex and appears to be required for normal structure and function of alpha-dystroglycan in muscle and brain
The authors report on a patient with Walker-Warburg syndrome and a novel POMT1 mutation. The patient expressed alpha-dystroglycan core protein, but fully glycosylated alpha-DG antibody epitopes were absent, associated with loss of laminin-binding activity
Results indicate that mutations in the protein O-mannosyltransferase 1 gene result in a defect of protein O-mannosylation in Walker-Warburg syndrome patients.
during embryogenesis, Pomt1 is expressed in the neural tube, the developing eye, and the mesenchyme; targeted deletion of Pomt1 results in early embryonic lethality due to defects in the assembly of Reichert's membrane
The protein encoded by this gene is an O-mannosyltransferase that requires interaction with the product of the POMT2 gene for enzymatic function. The encoded protein is found in the membrane of the endoplasmic reticulum. Defects in this gene are a cause of Walker-Warburg syndrome (WWS) and limb-girdle muscular dystrophy type 2K (LGMD2K). Several transcript variants encoding different isoforms have been found for this gene.
dolichyl-phosphate-mannose--protein mannosyltransferase 1
, dolichyl-phosphate-mannose-protein mannosyltransferase
, protein O-mannosyl-transferase 1
, protein O-mannosyltransferase 1