MilliporeSigma™ O-GlcNAc, Mouse, Unlabeled, Clone: RL1,
Manufacturer: MilliporeSigma™
Select a Size
| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| Each of 1 | MABS1253MI-Each-of-1 | In Stock | ₹ 42,968.31 |
MABS1253MI - Each of 1
In Stock
Quantity
1
Base Price: ₹ 42,968.31
GST (18%): ₹ 7,734.296
Total Price: ₹ 50,702.606
Antigen
O-GlcNAc
Classification
Monoclonal
Concentration
Please refer to lot specific datasheet.
Formulation
Purified mouse IgM in buffer containing PBS without preservatives.
Immunogen
Nuclear pore complex-lamina fraction isolated from rat liver nuclear envelopes.
Quantity
100 μL
Research Discipline
Signaling
Test Specificity
Both clone RL1 & clone RL2 (Mfr. No. MABS157) target O-linked N-acetylglucosamine (GlcNAc) modified (GlcNAcylated) proteins. GlcNAc removal by beta-N-acetylglucosaminidase treatment or galactosylation of GlcNAc on target proteins by galactosyltransferase treatment greatly reduced the immunoreactivity of clone RL1 & RL2 toward their target proteins. The binding affinity of RL1 and RL2 toward a given GlcNAcylated protein is dependent on both O-GlcNAc and the adjacent core protein structure (Snow, C.M., et al. (1987). J. Cell Biol. 104(5):1143-11560; Holt, G.D., et al. (1987). J. Cell Biol. 104(5):1157-1164).
Content And Storage
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze
Isotype
IgM κ
Applications
Immunoassay, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Inhibition Assays
Clone
RL1
Conjugate
Unconjugated
Host Species
Mouse
Purification Method
Purified by Ion-Exchange Chromatography
Regulatory Status
RUO
Primary or Secondary
Primary
Target Species
Drosophila
Form
Purified
Related Products
Description
- Posttranslational modification of proteins by -linked N-acetylglucosamine ( -GlcNAc) via the hydroxyl moieties on serine or threonine residues is termed O-linked -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.