Glycosylation of asparagine residues in Asn-X-Ser/Thr motifs in proteins commonly occur in the lumen of the endoplasmic reticulum (ER). Glucosidase I catalyzes the first step in the N-linked oligosaccharide processing pathway. It specifically removes the distal alpha 1,2-linked glucose residue from the Glc3-Man9-GlcNAc2 oligosaccharide precursor. Glucosidase I contains a short cytosolic tail, a single pass transmembrane domain and a large C-terminal catalytic domain located on the luminal side of the ER. Mutations in the gene encoding Glucosidase I result in the congenital disorder glycosylation (CDG-IIb), which is characterized by generalized hypotonia, dysmorphic features, hepatomegaly, hypoventilation, feeding problems, seizures and death. Two point mutations in the Glucosidase I gene have been identified and result in amino acid substitutions, namely Arg486Thr and Phe652Leu, that affect polypeptide folding and active site formation.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Glucosidase I of human origin by WB and ELISA
Tissue Specificity
recommended for detection of Glucosidase I of human origin by WB and ELISA