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Key Documents

O7764

Sigma-Aldrich

Anti-β-O-Linked N-Acetylglucosamine antibody, Mouse monoclonal

clone CTD110.6, purified from hybridoma cell culture

Synonym(s):

Anti-O-GLcNAc, Anti-OGT

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

CTD110.6, monoclonal

form

buffered aqueous solution

species reactivity

wide range

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 0.2-0.4 μg/mL using total cell extract of HeLa cells

isotype

IgM

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... OGT(8473)

General description

Monoclonal Anti-β-O-Linked N-Acetylglucosamine (mouse IgM isotype) is derived from the hybridoma CTD110.6 produced by the fusion of mouse myeloma cells (P3X63-Ag8.653 cells) and cells from BALB/c mice immunized with a synthetic peptide YSPTS(O-GlcNAc)PSK conjugated to KLH. This antibody recognizes O-GlcNAc in β-O-glycosidic linkage to both serine and threonine and does not cross react with α-linked Ser/Thr-O-GlcNAc, α-linked Ser-O-linked N-acetylgalactosamine or N-linked oligosaccharides on ovalbumin and immunoglobulin G. O-linked N-acetylglucosamine (GlcNAc) transferase (OGT) has 13.5 tetratricopeptide-repeats (TPR) and a globular catalytic domain. The gene encoding this protein is localized on human chromosome Xq13.1.

Specificity

The antibody recognizes O-GlcNAc in β-O-glycosidic linkage to both serine and threonine and does not cross reacts with α-linked Ser/Thr-O-GlcNAc, α-linked Ser-O-linked N-acetylgalactosamine or N-linked oligosaccharides on ovalbumin and immunoglobulin G.

Immunogen

synthetic peptide YSPTS(O-GlcNAc)PSK.

Application

Monoclonal Anti-β-O-Linked N-Acetylglucosamine antibody produced in mouse has been used in Western Blotting.

Biochem/physiol Actions

O-linked N-acetylglucosamine (GlcNAc) transferase (OGT) has a role in the addition of O-linked N-acetylglucosamine (O-GlcNAc) to serine/threonine residues in the protein of interest. It is crucial for O-GlcNAcylation of RNA polymerase II. Absence of OGT has been shown to reduce transcription and pol II promoter occupancy. The gene is upregulated in breast cancer tissues, colon cancer, lung cancer and laryngeal cancer. This protein might be associated with tumorigenesis and metastasis.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Disclaimer

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

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Human RNA Polymerase II Promoter Recruitment in Vitro Is Regulated by O-Linked N-Acetylglucosaminyltransferase (OGT).
Lewis BA
The Journal of Biological Chemistry, 291(27, 14056-14061 (2016)
F I Comer et al.
Analytical biochemistry, 293(2), 169-177 (2001-06-12)
beta-O-linked N-acetylglucosamine (O-GlcNAc) is an abundant posttranslational modification of resident nuclear and cytoplasmic proteins in eukaryotes. Increasing evidence suggests that O-GlcNAc plays a regulatory role in numerous cellular processes. Here we report on the production and characterization of a highly
Silencing ?-linked N-acetylglucosamine transferase induces apoptosis in human gastric cancer cells through PUMA and caspase-3 pathways.
Wen T
Oncology Reports, 34(6), 3140-3146 (2015)
Antibodies That Detect O-Linked ?-D-N-Acetylglucosamine on the Extracellular Domain of Cell Surface Glycoproteins*
Yuko Tashima and Pamela Stanley
The Journal of Biological Chemistry, 289, 1132-1142 (2014)
Distinct OGT-Binding Sites Promote HCF-1 Cleavage.
Bhuiyan T
PLoS ONE, 10(8), e0136636-e0136636 (2015)

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