
Thermo Fisher Scientific O-GlcNAc Monoclonal Antibody (RL2), Alexa Fluor 647, eBioscience
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Applications
Tested Dilution
Publications
Flow Cytometry (Flow)
5 µL (0.5 µg)/test
Product Specifications
Host/Isotype
Mouse / IgG1, kappa
Recommended Isotype Control
Mouse IgG1 kappa Isotype Control (P3.6.2.8.1), Alexa Fluor™ 647, eBioscience™
Class
Monoclonal
Type
Antibody
Clone
RL2
Immunogen
Rat liver nuclear envelopes
Conjugate
Alexa Fluor™ 647 Alexa Fluor™ 647 Alexa Fluor™ 647
View additional formats
Excitation/Emission Max
650/671 nm View spectra
Form
Liquid
Concentration
5 µL/Test
Storage conditions
4° C, store in dark, DO NOT FREEZE!
Shipping conditions
Wet ice
RRID
AB_2784742
Product Specific Information
Description: This RL2 monoclonal antibody recognizes proteins with O-N-acetylglucosamine (O-GlcNAc) glycosylation. It was originally developed by immunizing mice with the rat liver nuclear envelopes containing nuclear pore complexes. The RL2 clone has been successfully used in Western blot, immunofluorescence, immunoprecipitation, and flow cytometry in a wide variety of mammalian cells.
Applications Reported: This RL2 antibody has been reported for use in intracellular staining followed by flow cytometric analysis.
Applications Tested: This RL2 antibody has been pre-diluted and tested by intracellular staining followed by flow cytometric analysis of normal human peripheral blood cells using the Foxp3/Transcription Factor Staining Buffer Set (Product # 00-5523-00) and protocol. Please refer to BestProtocols®: Protocol B: One step protocol for (nuclear) intracellular proteins located under the Resources Tab online. This may be used at 5 µL (0.5 µg) per test. A test is defined as the amount (µg) of antibody that will stain a cell sample in a final volume of 100 µL. Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test.
Excitation: 633-647 nm; Emission: 668 nm; Laser: Red Laser.
Target Information
O-linked N-acetylglucosamine (O-GlcNAc) is a posttranslational modification characterized by the attachment of N-acetylglucosamine to specific serine or threonine residues. Unlike other protein glycosylations, O-GlcNAc modifications occur within the nucleus and cytoplasm. They are found on many cellular proteins, including nuclear pore, oncogene, cytoskeletal, heat shock, viral and transcription regulatory proteins. O-GlcNAc glycosylations are thought to obscure phosphorylation sites, counteracting phosphorylation-dependent signaling pathways and protein interactions.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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