• Product name

  • Description

    Rabbit polyclonal to UGGT/UGT1
  • Host species

  • Tested applications

    Suitable for: IP, WBmore details
  • Species reactivity

    Reacts with: Mouse, Human
  • Immunogen

    Synthetic peptide within Human UGGT/UGT1 aa 1505-1555. The exact sequence is proprietary.
    Database link: Q9NYU2

  • Positive control

    • WB:HeLa, HEK-293T, Jurkat, TCMK-1 and NIH/3T3 whole cell lysates. IP: HEK-293T whole cell lysate.
  • General notes

     This product was previously labelled as UGGT



  • Form

  • Storage instructions

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
  • Storage buffer

    Preservative: 0.09% Sodium azide
    Constituent: Tris citrate/phosphate

    pH 7 to 8
  • Concentration information loading...
  • Purity

    Immunogen affinity purified
  • Purification notes

    Antibody was affinity purified using an epitope specific to UGGT/UGT1 immobilized on solid support.
  • Clonality

  • Isotype

  • Research areas


Our Abpromise guarantee covers the use of ab241357 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
IP Use at 2-10 µg/mg of lysate.
WB 1/2000 - 1/10000. Predicted molecular weight: 177 kDa.


  • Function

    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.
  • Tissue specificity

    Higher levels in pancreas, skeletal muscle, kidney, and brain. Low levels in lung and heart.
  • Pathway

    Protein modification; protein glycosylation.
  • Sequence similarities

    Belongs to the glycosyltransferase 8 family.
  • Domain

    The N-terminal non-catalytic domain is assumed to mediate recognition of proteins with partial folding defects.
  • Cellular localization

    Endoplasmic reticulum lumen. Endoplasmic reticulum-Golgi intermediate compartment.
  • Information by UniProt
  • Database links

  • 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
    see all


  • All lanes : Anti-UGGT/UGT1 antibody (ab241357) at 0.1 µg/ml

    Lane 1 : HeLa (human epithelial cell line from cervix adenocarcinoma) whole cell lysate
    Lane 2 : HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate
    Lane 3 : Jurkat (human T cell leukemia cell line from peripheral blood) whole cell lysate
    Lane 4 : TCMK-1 (mouse kidney epithelial cell line) whole cell lysate
    Lane 5 : NIH/3T3 (mouse embryo fibroblast cell line) whole cell lysate

    Lysates/proteins at 15 µg per lane.

    Developed using the ECL technique.

    Predicted band size: 177 kDa

    Exposure time: 10 seconds

    Lysates prepared in NETN buffer.

  • UGGT/UGT1 was immunoprecipitated from HEK-293T (human epithelial cell line from embryonic kidney transformed with large T antigen) whole cell lysate (1 mg for IP, 20% of IP loaded) with ab241357 at 6 µg/reaction. Western blot was performed from the immunoprecipitate using ab241357 at 1 µg/ml.

    Lane 1: ab241357 IP in HEK-293T whole cell lysate.
    Lane 2: Control IgG IP in HEK-293T whole cell lysate.

    Detection: Chemiluminescence with exposure time of 30 seconds.

    Lysates prepared in NETN buffer.


ab241357 has not yet been referenced specifically in any publications.

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