Uridine diphosphate (UDP)-glucose:glycoprotein glucosyltransferase 1 (UGGT1) is a large soluble protein of the endoplasmic reticulum (ER). It contains a N-terminal folding sensor domain and a C-terminal catalytic domain that transfers glucose residues. It is a member of the glycosyltransferase family 24.
Specificity
Anti-UGGT1 (mouse) recognizes mouse and rat UGGT1.
Immunogen
synthetic peptide corresponding to the C-terminal region of mouse UGGT1, conjugated to KLH. The corresponding sequence differs by one amino acid in rat.
Application
Anti-UGGT1 (mouse) antibody produced in rabbit may be used in immunoblotting.
Biochem/physiol Actions
Uridine diphosphate (UDP)-glucose:glycoprotein glucosyltransferase 1 (UGGT1) that selectively re-glucosylates unfolded glycoproteins, thus providing quality control for protein transport out of the endoplasmic reticulum (ER). It re-glucosylates incompletely folded glycoproteins to monoglucosylated intermediates. Re-glucosylated proteins are recognized by ER-resident carbohydrate-binding molecular chaperons, calnexin or calreticulin for recycling to the endoplasmic reticulum and refolding or degradation.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
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The Journal of cell biology, 189(5), 829-841 (2010-05-26)
An endoplasmic reticulum (ER) quality control system assists in efficient folding and disposal of misfolded proteins. N-linked glycans are critical in these events because their composition dictates interactions with molecular chaperones. UDP-glucose:glycoprotein glucosyltransferase 1 (UGT1) is a key quality control
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