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The protein encoded by B3GALTL is a beta-1,3-glucosyltransferase that transfers glucose to O-linked fucosylglycans on thrombospondin type-1 repeats (TSRs) of several proteins. Additionally we are shipping B3GALTL Kits (14) and B3GALTL Proteins (7) and many more products for this protein.
Showing 10 out of 19 products:
Human Polyclonal B3GALTL Primary Antibody for IHC, ELISA - ABIN1534691
Sato, Sato, Kiyohara, Sogabe, Shikanai, Kikuchi, Togayachi, Ishida, Ito, Kameyama, Gotoh, Narimatsu et al.: Molecular cloning and characterization of a novel human beta1,3-glucosyltransferase, which is localized at the endoplasmic reticulum and glucosylates O-linked fucosylglycan on thrombospondin type 1 ... in Glycobiology 2006
Show all 2 references for ABIN1534691
Human Polyclonal B3GALTL Primary Antibody for WB - ABIN2783666
Hess, Keusch, Oberstein, Hennekam, Hofsteenge: Peters Plus syndrome is a new congenital disorder of glycosylation and involves defective Omicron-glycosylation of thrombospondin type 1 repeats. in The Journal of biological chemistry 2008
POFUT2 (show POFUT2 Antibodies) and B3GLCT mediate a noncanonical endoplasmic reticulum quality-control mechanism that recognizes folded thrombospondin type 1 repeats and stabilizes them by glycosylation.
Mutations in the coding region of B3GALTL were identified in nine patients; six had a documented phenotype of classic Peters plus syndrome (PPS) and the remaining three had a clinical diagnosis of PPS with incomplete clinical documentation.
a novel c.597-2 A>G splicing mutation within the B3GALTL gene in typical Peters-plus syndrome
A novel homozygous c.597-2A>G mutation was identified in both patients with Peters plus syndrome harbouring a novel splice site mutation in the B3GALTL gene
Vertebral defects in a patient with Peters plus syndrome and mutations in B3GALTL.
The present report confirms the wide clinical spectrum of Peters plus syndrome, underlines the major clinical criteria of the syndrome and the major implication of B3GALTL gene in this condition.
Novel B3GALTL mutation in Peters-plus Syndrome
B3GTL is transcribed in a wide range of tissues and has conserved domains and motifs
We report here the molecular cloning and characterization of a novel beta1,3-glucosyltransferase (beta3Glc-T) that synthesizes a Glcbeta1,3Fucalpha- structure on the TSR (show CFL1 Antibodies) domain.
Biallelic truncating mutations in the beta 1,3-galactosyltransferase-like gene (B3GALTL) in all 20 tested patients, showed that Peters Plus is a monogenic, primarily single-mutation syndrome.
The protein encoded by this gene is a beta-1,3-glucosyltransferase that transfers glucose to O-linked fucosylglycans on thrombospondin type-1 repeats (TSRs) of several proteins. The encoded protein is a type II membrane protein. Defects in this gene are a cause of Peters-plus syndrome (PPS).
, beta 3-glycosyltransferase-like
, UDP-GAL:beta-GlcNAc beta-1,3-galactosyltransferase-like