UGGT1 Antibody

Code CSB-PA025565GA01HU
Size $600
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Product Details

Uniprot No.
Target Names
Alternative Names
GT antibody; HUGT1 antibody; UDP glucose glycoprotein glucosyltransferase 1 antibody; UDP Glucose Glycoprotein Glucosyltransferase antibody; UDP--Glc:glycoprotein glucosyltransferase antibody; UDP-glucose ceramide glucosyltransferase-like 1 antibody; UDP-glucose:glycoprotein glucosyltransferase 1 antibody; UGCGL1 antibody; UGGG1 antibody; UGGG1_HUMAN antibody; UGGT antibody; Uggt1 antibody; UGT1 antibody; UGTR antibody
Raised in
Species Reactivity
Human UGCGL1
Immunogen Species
Homo sapiens (Human)
Purification Method
Antigen Affinity purified
It differs from different batches. Please contact us to confirm it.
PBS with 0.1% Sodium Azide, 50% Glycerol, pH 7.3. -20°C, Avoid freeze / thaw cycles.
Tested Applications
Troubleshooting and FAQs
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation.
Gene References into Functions
  1. both vIL-6 and VKORC1v2 interact with calnexin cycle proteins UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), which catalyzes monoglucosylation of N-glycans, and oppositely acting glucosidase II (GlucII), and that vIL-6 can promote protein folding. PMID: 28878084
  2. These findings provide important insight on the role of unfolded protein response (UPR) and host UGGT1 in regulating RNA virus replication and pathogenicity. PMID: 28545059
  3. The results demonstrated that FAM5C is an N-glycosylated protein, and N-glycosylation by UGGT1 is necessary for the secretion of FAM5C. PMID: 28351617
  4. A novel UGGT1- and p97-dependent protein quality checkpoint is shown. This checkpoint is alerted to prevent secretion of a polypeptide that passes the luminal quality control scrutiny by BiP and CNX but contains an intramembrane ionizable residue. PMID: 25694454
  5. Kyte-Doolittle analysis as well as homology modeling revealed a cluster of hydrophobic amino acids that may be functional in the folding sensing mechanism of HUGT1 PMID: 26196150
  6. Results indicate that glycan structures are similar to endogenous glycans at low expression levels of uridine 5'-diphosphate-glucose: glycoprotein glucosyltransferase (UGGT1). PMID: 25935482
  7. The UGGT1 is a well-documented enzyme which functions as a folding sensor in the endoplasmic reticulum, by the virtue of its ability to transfer a glucose residue to non-glucosylated high-mannose-type glycans of immature glycoproteins. PMID: 24415556
  8. UGT1 aids in the folding of sequential domain-containing proteins such as prosaposin. PMID: 20498017
  9. The substrate binding specificity PMID: 12682060
  10. the amino-terminal 80% of HUGT1 is required for activation of the catalytic domain PMID: 12913004
  11. overexpression leads to increase in production of recombinant proteins; gene targeting PMID: 19466607

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Subcellular Location
Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment.
Protein Families
Glycosyltransferase 8 family
Tissue Specificity
Higher levels in pancreas, skeletal muscle, kidney, and brain. Low levels in lung and heart.
Database Links

HGNC: 15663

OMIM: 605897

KEGG: hsa:56886

STRING: 9606.ENSP00000259253

UniGene: Hs.743306

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