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Key Specifications Table
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| A | WB, ELISA, IP | M | Purified | Monoclonal Antibody |
| Description | |
|---|---|
| Catalogue Number | MABS1254 |
| Description | Anti-O-GlcNAc Antibody, clone CTD110.6 |
| Alternate Names |
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| Background Information | Posttranslational modification of proteins by β-linked N-acetylglucosamine (β-GlcNAc) via the hydroxyl moieties on serine or threonine residues is termed O-linked β-GlcNAc or simply O-GlcNAc. O-GlcNAc is one of the most abundant posttranslational modifications within the nucleocytoplasmic compartments of all animals and plants. Unlike other types of protein glycosylations, O-GlcNAc occurs exclusively within the nuclear and cytoplasmic compartments and is generally not further modified to form more elongated structures. In addition, O-GlcNAcylation is a highly dynamic and reversible process. The O-GlcNAc transferase (OGT) attaches O-GlcNAc to proteins at specific serine or threonine residues, while O-GlcNAcase catalyzes the removal/hydrolysis of O-GlcNAc from proteins. In fact, a dynamic interplay between O-GlcNAcylation and serine/threonine phosphorylation plays an important role in regulating cellular signaling. Tau and RNA polymerase II (Pol II) are two well known proteins that undergo modification by O-GlcNAcylation. In Alzheimer’s diseased human brains, tau becomes extensively phosphorylated and less O-GlcNAcylated. Similarly, O-GlcNAc is removed and replaced with O-phosphate on the Poly II CTD when the elongation phase of transcription is initiated. |
| Product Information | |
|---|---|
| Format | Purified |
| Presentation | Purified mouse monoclonal IgMκ antibody in PBS with 0.05% sodium azide. |
| Quality Level | MQ100 |
| Applications | |
|---|---|
| Application | Anti-O-GlcNAc Antibody, clone CTD110.6 is an antibody against O-GlcNAc for use in Western Blotting, ELISA, Immunoprecipitation. |
| Key Applications |
|
| Application Notes | Western Blotting Analysis: 1.0 µg/mL from a representative lot detected O-GlcNAcylated proteins in 7.5-15 µg of wild-type mouse embryonic fibroblast (MEF) lysate, but not O-GlcNAc transferase/OGT-deficient MEF lysate (Courtesy of Dr. Natasha Zachara and Gokben Yildirir, M.S.). ELISA Analysis: A representative lot detected RNA polymerase II C-terminal domain (CTD) peptide (YSPTSPS) with a single O-GlcNAcylated serine or threonine, but not the corresponding unmodified peptide (Comer, F.I., et al. (2001). Anal. Biochem. 293(2):169-177). Immunoprecipitation Analysis: A representative lot immunoprecipitated O-GlcNAcylated proteins from human pluripotent stem cells (hPSCs) (Maury, J.J., et al. (2013). Stem Cell Res. 11(2):926-937). Immunoprecipitation Analysis: A representative lot immunoprecipitated O-GlcNAcylated proteins from HeLa cell extracts (Comer, F.I., et al. (2001). Anal. Biochem. 293(2):169-177). Western Blotting Analysis: A representative lot detected similar level of cellular O-GlcNAcylation in undifferentiated, differentiating and terminally differentiated human pluripotent stem cells (hPSCs) (Maury, J.J., et al. (2013). Stem Cell Res. 11(2):926-937). Western Blotting Analysis: A representative lot detected BSA-conjugated RNA polymerase II C-terminal domain (CTD) peptide (YSPTSPS) with beta-O-linked GlcNAc, but not alpha-O-linked GlcNAc, nor the corresponding unmodified peptide. The presence of GlcNAc, but not GalNAc, abolished the detection of the target bands (Comer, F.I., et al. (2001). Anal. Biochem. 293(2):169-177). Western Blotting Analysis: A representative lot detected O-GlcNAcylated proteins in HeLa nuclear extract, as well as O-GlcNAcylated proteins purified from HeLa nuclear & cytosolic extract by wheat germ agglutinin (WGA) column. Antibody blocking by mmunogen peptide prior to immunoblotting abolished target bands detection (Comer, F.I., et al. (2001). Anal. Biochem. 293(2):169-177). Western Blotting Analysis: A representative lot detected an upregulation of O-GlcNAcylated proteins in Jurkat cells treated with the glucosaminidase inhibitor PUGNAc and the hexosamine pathway intermediate glucosamine (Comer, F.I., et al. (2001). Anal. Biochem. 293(2):169-177). |
| Biological Information | |
|---|---|
| Immunogen | KLH-conjugated peptide with an O-GlcNAc-modified serine residue. |
| Epitope | beta-O-linked GlcNAc. |
| Clone | CTD110.6 |
| Concentration | Please refer to lot specific datasheet. |
| Host | Mouse |
| Specificity | Clone CTD110.6 specifically detected serine and threonine residues with beta-O-linked GlcNAc, but not alpha-O-linked GlcNAc. The presence of GlcNAc, but not GalNAc, abolished the detection of the target modification. Clone CTD110.6 did not recognize peptides with unmodified serine and threonine residues (Comer, F.I., et al. (2001). Anal. Biochem. 293(2):169-177). |
| Isotype | IgMκ |
| Species Reactivity |
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| Species Reactivity Note | All Species. Target modification is not species-specific. |
| Antibody Type | Monoclonal Antibody |
| Entrez Gene Number |
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| Gene Symbol |
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| UniProt Number |
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| Molecular Weight | Variable, depending on the size(s) of the O-GlcNAcylated protein(s). |
| Product Usage Statements | |
|---|---|
| Quality Assurance | Evaluated by Western Blotting in HeLa cell lysate. Western Blotting Analysis: 4.0 µg/mL of this antibody detected O-GlcNAcylated proteins in 10 µg of HeLa cell lysate. |
| Usage Statement |
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| Storage and Shipping Information | |
|---|---|
| Storage Conditions | Stable for 1 year at 2-8°C from date of receipt. |
| Packaging Information | |
|---|---|
| Material Size | 100 µL |