MABS157
Anti-O-Linked N-Acetylglucosamine Antibody, clone RL2
clone RL2, from mouse
Synonym(s):
O-Linked N-Acetylglucosamine
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All Photos(2)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
RL2, monoclonal
species reactivity (predicted by homology)
all
technique(s)
affinity binding assay: suitable
electron microscopy: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1κ
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... OGT(8473)
General description
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.
Specificity
Specifically recoginzes O-linked N-Acetylglucosamine (O-GlcNAc) moieties on O-GlcNAcylated proteins and peptides. Exhibits little reactivity toward free GIcNAc and no reactivity toward GalNac. Galactosyltransferase treatment of O-GlcNAcylated proteins results in galactosylation of O-GlcNAc via β1-4 linkage and a complete loss of binding by clone RL2 (Holt, G.D., et al. (1987). J. Cell Biol. 104(5):1157-1164).
Target structure is not species-specific.
Immunogen
Pore complex-lamina fraction purified from rat liver nuclear envelopes corresponding to Rat O-Linked N-Acetylglucosamine.
Application
Anti-O-Linked N-Acetylglucosamine Antibody, clone RL2 is an antibody against O-Linked N-Acetylglucosamine for use in Western Blotting, Immunocytochemistry, Affinity Binding Assay, Electron Microscopy, Immunoprecipitation.
Immunocytochemistry Analysis: 4.0 µg/mL from a representative lot detected O-Linked N-Acetylglucosamine in HeLa cells.
Immunocytochemistry Analysis: A representative lot immunostained nuclear envelopes, but not the nuclear interior, of digitonin-permeabilized HeLa cells. Clone RL2 stained the nuclear interior only among Triton X-100-permeabilized HeLa cells without intact nuclear envelopes (Adam, S.A., et al. (1990). J. Cell Biol. 111(3):807-816).
Affinity Binding Assay: A representative lot was radiolabeled with 125I and studied for its binding characteristics toward isolated rat liver nuclear envelopes (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156).
Electron Microscopy: A representative lot localized the O-GlcNAc immunoreactivity in isolated rat liver nuclear envelopes (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156).
Western Blotting Analysis: A representative lot detected O-GlcNAcylated proteins in rat liver nuclear envelopes preparations (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156; Holt, G.D., et al. (1987). J. Cell Biol. 104(5):1157-1164).
Immunoprecipitation Analysis: A representative lot immunoprecipitated O-GlcNAcylated proteins from solubilized rat liver nuclear envelopes preparations. Pretreatment of nuclear envelopes preparations with galactosyltrarnsferase prevented the immunoprecipitation of glycoproteins by clone RL2 (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156; Holt, G.D., et al. (1987). J. Cell Biol. 104(5):1157-1164).
Immunocytochemistry Analysis: A representative lot immunostained nuclear envelopes, but not the nuclear interior, of digitonin-permeabilized HeLa cells. Clone RL2 stained the nuclear interior only among Triton X-100-permeabilized HeLa cells without intact nuclear envelopes (Adam, S.A., et al. (1990). J. Cell Biol. 111(3):807-816).
Affinity Binding Assay: A representative lot was radiolabeled with 125I and studied for its binding characteristics toward isolated rat liver nuclear envelopes (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156).
Electron Microscopy: A representative lot localized the O-GlcNAc immunoreactivity in isolated rat liver nuclear envelopes (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156).
Western Blotting Analysis: A representative lot detected O-GlcNAcylated proteins in rat liver nuclear envelopes preparations (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156; Holt, G.D., et al. (1987). J. Cell Biol. 104(5):1157-1164).
Immunoprecipitation Analysis: A representative lot immunoprecipitated O-GlcNAcylated proteins from solubilized rat liver nuclear envelopes preparations. Pretreatment of nuclear envelopes preparations with galactosyltrarnsferase prevented the immunoprecipitation of glycoproteins by clone RL2 (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-1156; Holt, G.D., et al. (1987). J. Cell Biol. 104(5):1157-1164).
Quality
Evaluated by Western Blotting in HeLa cell lysate.
Western Blotting Analysis: 1.0 µg/mL of this antibody detected O-Linked N-Acetylglucosamine in 10 µg of HeLa cell lysate.
Western Blotting Analysis: 1.0 µg/mL of this antibody detected O-Linked N-Acetylglucosamine in 10 µg of HeLa cell lysate.
Target description
Variable, depending on the size(s) of the O-GlcNAcylated protein(s).
Physical form
Format: Purified
Other Notes
Concentration: Please refer to lot specific datasheet.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Listings
Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.
JAN Code
MABS157:
Certificates of Analysis (COA)
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Find documentation for the products that you have recently purchased in the Document Library.
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
Snow, CM; Senior, A; Gerace, L
The Journal of cell biology null
Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors.
Adam, SA; Marr, RS; Gerace, L
The Journal of cell biology null
Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine.
Holt, GD; Snow, CM; Senior, A; Haltiwanger, RS; Gerace, L; Hart, GW
The Journal of cell biology null
Jin-Wei Jhu et al.
International journal of molecular sciences, 22(18) (2021-09-29)
Glutamine and lipids are two important components of proliferating cancer cells. Studies have demonstrated that glutamine synthetase (GS) boosts glutamine-dependent anabolic processes for nucleotide and protein synthesis, but the role of GS in regulating lipogenesis remains unclear. This study identified
Ilaria Zuliani et al.
International journal of molecular sciences, 22(7) (2021-05-01)
The disturbance of protein O-GlcNAcylation is emerging as a possible link between altered brain metabolism and the progression of neurodegeneration. As observed in brains with Alzheimer's disease (AD), flaws of the cerebral glucose uptake translate into reduced protein O-GlcNAcylation, which
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