Thermo Fisher Scientific O-linked N-acetylglucosamine (O-GlcNAc) Monoclonal Antibody (HGAC85)

Applications

Tested Dilution

Publications

Western Blot (WB)

1:250-1:1,000

View 7 publications 7 publications

Immunohistochemistry (IHC)

-

View 3 publications 3 publications

Immunocytochemistry (ICC/IF)

1:250

View 3 publications 3 publications

ELISA (ELISA)

Assay-dependent

View 1 publication 1 publication

Immunoprecipitation (IP)

Assay-dependent

View 4 publications 4 publications

ChIP assay (ChIP)

-

View 3 publications 3 publications

Product Specifications

Species Reactivity

Chemical

Published species

Chemical, Fruit fly, Hamster, Human, Mouse, Nematode, Rabbit, Rat, Sheep

Host/Isotype

Mouse / IgG3

Class

Monoclonal

Type

Antibody

Clone

HGAC85

Immunogen

Heat killed, pepsin treated group A streptococci.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

Conc. Not Determined

Storage buffer

ascites, PBS

Contains

0.05% sodium azide

Storage conditions

-20° C, Avoid Freeze/Thaw Cycles

Shipping conditions

Wet ice

RRID

AB_326365

Product Specific Information

MA1-076 recognizes beta-1,3 linked O-linked N-acetylglucosamine (O-GlcNAc) residues of streptococcal group A carbohydrate as well as O-GlcNAc glycosylated proteins.

MA1-076 has been successfully used in Western blot, immunofluorescence, immunoprecipitation and ELISA procedures. By Western blot, this antibody detects several proteins representing immunoprecipitated O-GlcNAc glycoproteins. Immunofluorescence staining of O-GlcNAc in cells results in labeling of the nuclear envelope and pores, nucleolus, and cytoplasm. This staining pattern is consistent with other methods of detecting O-GlcNAc moieties.

The MA1-076 immunogen is heat killed, pepsin treated group A streptococci.

DO NOT USE WITH DILUENTS CONTAINING GLYCOSYLATED PROTEINS.

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.