biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~130 kDa
species reactivity
human, mouse, canine
concentration
~1.5 mg/mL
technique(s)
indirect immunofluorescence: 5-10 μg/mL using A431 cells, western blot: 1.5-3.0 μg/mL using MDCK and mouse kidney extracts.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... MGEA5(10724)
mouse ... Mgea5(76055)
rat ... Mgea5(154968)
Immunogen
synthetic peptide corresponding to a sequence located near the N-terminus of human O-GlcNAcase (OGA), conjugated to KLH. The corresponding sequence is identical in human OGA isoform B, and in rat and mouse OGA.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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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存储类别
12 - Non Combustible Liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
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相关内容
Instructions
Fuxing Zhou et al.
Theranostics, 8(19), 5200-5212 (2018-12-18)
Cisplatin resistance significantly affects the survival rate of patients with ovarian cancer. However, the main mechanism underlying cisplatin resistance in ovarian cancer remains unclear. Methods: Immunohistochemistry was used to determine the expression of OGT, OGA and O-GlcNAc in chemoresistant and
Villo Muha et al.
The Journal of biological chemistry, 295(26), 8636-8646 (2020-02-26)
O-GlcNAcylation is an abundant post-translational modification in neurons. In mice, an increase in O-GlcNAcylation leads to defects in hippocampal synaptic plasticity and learning. O-GlcNAcylation is established by two opposing enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). To investigate the role
Sung-Kyun Park et al.
Cell reports, 20(5), 1088-1099 (2017-08-03)
Modification of nucleocytoplasmic proteins with O-GlcNAc regulates a wide variety of cellular processes and has been linked to human diseases. The enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) add and remove O-GlcNAc, but the mechanisms regulating their expression remain unclear.