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Description
Trip230 was identified as a protein that interacts with retinoblastoma protein (Rb) and the thyroid hormone receptor (TR). The structure of Trip230 includes five coiled-coil segments separated by non-helical linkers, N-terminal and C-terminal leucine zipper domains, and multiple phosphorylation sites. Trip230 is ubiquitously expressed and localized to the Golgi. During cell cycle progression, a significant portion of Trip230 translocates to the nucleus. In addition, activation of TR with thyroid hormone (T3) leads to phosphorylation of Trip230, as well as Trip230 translocation from the Golgi to the nucleus. Interestingly, Trip230 has also been identified as a Golgi microtubule-associated protein of 210kDa (GMAP-210). In vitro , GMAP-210 can bind to the minus end of α-tubulin and γ-tubulin via its C-terminal region, while the N-terminal region is involved in Golgi binding. Overexpression of GMAP-210 leads to enlargement of the Golgi apparatus and alterations in the microtubule cytoskeleton. Thus, GMAP-210/Trip230 is thought to function both as a TR coactivator and as a microtubule-binding protein that anchors the Golgi to the microtubule cytoskeleton.
Host Species: Mouse
Clone: 15
Isotype: IgG1
Species Reactivity [for Features Main]: Human
Immunogen: Human GMAP-210 aa. 159-365
Immunofluorescence, Western Blotting
Specifications
Specifications
| Antigen | GMAP-210 (Trip230) |
| Applications | Western Blot |
| Classification | Monoclonal |
| Clone | 15 |
| Concentration | 250μg/mL |
| Conjugate | Unconjugated |
| Description | Trip230 |
| Formulation | Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Human GMAP-210 aa. 159-365 |
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