Product Details
| Clone: | GX41 |
| |
| Host: | Mouse |
| |
| Isotype: | IgG1κ |
| |
| Immunogen: | Diglycine-modified histone from calf thymus, Type III-S, lysine rich fraction. |
| |
| Source: | Purified from hybridoma tissue culture supernatant. |
| |
| Species reactivity: | Species independent
|
| |
| Specificity: | Recognizes diglycyl modified lysine, a ubiquitin remnant detectable after trypsin digestion. |
| |
| Applications: | IP, WB
|
| |
| Purity Detail: | Protein G purified. |
| |
| Formulation: | Liquid. In PBS containing 0.1% sodium azide. |
| |
| Handling: | Store unopened vial at -20°C until required for use. Store diluted antibody at 2-4°C and use within 1 month. Avoid freeze/thaw cycles. |
| |
| Shipping: | Blue Ice |
| |
| Long Term Storage: | -20°C |
| |
| Scientific Background: | Protein ubiquitination is a fundamentally important post-translational modification that regulates myriad cell signaling pathways in eukaryotes. Alterations in protein ubiquitination have been linked to cancers and neurodegenerative, cardiovascular, immunological, and inflammatory diseases.
Identification of exact ubiquitinylation sites is challenging under physiological conditions, but the recent development of an immunoprecipitation approach allows for enrichment and identification of peptides derived from the ubiquitinated portion of proteins.
When ubiquitinated protein is digested with trypsin a diglycine residue remains at any lysine site of ubiquitin attachment. Diglycyl Lysine, mAb (GX41) facilitates easy capture and enrichment of peptides derived from ubiquitinated proteins by recognizing the diglycyl-lysine residue with no detectable reactivity to non modified lysines. |
| |
| Regulatory Status: | RUO - Research Use Only |
| |
Product Literature References
Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues: S.A. Wagner, et al.; Mol. Cell. Proteomics
11, 1578 (2012),
Abstract;
Full Text
Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass: L.K. Povlsen, et al.; Nat. Cell Biol.
14, 1089 (2012),
Abstract;
A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles: S.A. Wagner, et al.; Mol. Cell. Proteomics
10, M111.013284 (2011),
Abstract;
Full Text
The new landscape of protein ubiquitination: G. Xu, et al.; Nat. Biotechnol.
290, 1098 (2011),
Abstract;
Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling: G. Xu, et al.; Nat. Biotechnol.
28, 868 (2010),
Abstract;
Full Text
