추천 제품
일반 설명
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.
특이성
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).
Target modification is not species-specific.
면역원
Epitope: beta-O-linked GlcNAc.
KLH-conjugated peptide with an O-GlcNAc-modified serine residue.
애플리케이션
Anti-O-GlcNAc Antibody, clone CTD110.6 is an antibody against O-GlcNAc for use in Western Blotting, ELISA, Immunoprecipitation.
Research Category
Signaling
Signaling
Research Sub Category
General Post-translation Modification
General Post-translation Modification
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).
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).
품질
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.
Western Blotting Analysis: 4.0 µg/mL of this antibody detected O-GlcNAcylated proteins in 10 µg of HeLa cell lysate.
표적 설명
Variable, depending on the size(s) of the O-GlcNAcylated protein(s).
물리적 형태
Format: Purified
Purified mouse monoclonal IgMκ antibody in PBS with 0.05% sodium azide.
저장 및 안정성
Stable for 1 year at 2-8°C from date of receipt.
기타 정보
Concentration: Please refer to lot specific datasheet.
면책조항
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
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Journal of the American Chemical Society, 144(2), 832-844 (2022-01-06)
Owing to its roles in human health and disease, the modification of nuclear, cytoplasmic, and mitochondrial proteins with O-linked N-acetylglucosamine residues (O-GlcNAc) has emerged as a topic of great interest. Despite the presence of O-GlcNAc on hundreds of proteins within
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