RanGAP1 (D2T7T) Rabbit mAb #36067
- WB
- IP
- eCLIP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 68, 82 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- eCLIP-eCLIP
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| eCLIP | 1:200 |
Storage
Protocol
Specificity / Sensitivity
RanGAP1 (D2T7T) Rabbit mAb recognizes endogenous levels of total RanGAP1 protein. This antibody detects unmodified and SUMO-1 modified RanGAP1 protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human RanGAP1 protein.
Background
Ran GTPase activating protein 1 (RanGAP1) regulates GTP hydrolysis by Ran, which is required for the ability of Ran to regulate nucleocytoplasmic shuttling (1). A significant fraction of cellular RanGAP1 is covalently modified by SUMO-1, which is required for relocalization of RanGAP1from the cytoplasm to the nuclear pore complex and the mitotic spindle (2-5). Research studies demonstrate that RanGAP1 sumoylation is required for stable association of RanGAP1 with RanBP2. Together with the SUMO-conjugating enzyme UBC9/UBE2I, RanGAP1 and RanBP2 are part of a SUMO E3 ligase complex that is implicated in regulating nucleocytoplasmic protein trafficking (6-8). Phosphorylation of RanGAP1 occurs in a cell-cycle-dependent manner and may play a role in regulating RanGAP1 catalytic activity (9,10).
- Bischoff, F.R. et al. (1994) Proc Natl Acad Sci U S A 91, 2587-91.
- Mahajan, R. et al. (1997) Cell 88, 97-107.
- Matunis, M.J. et al. (1998) J Cell Biol 140, 499-509.
- Matunis, M.J. et al. (1996) J Cell Biol 135, 1457-70.
- Joseph, J. et al. (2002) J Cell Biol 156, 595-602.
- Hutten, S. et al. (2008) Mol Biol Cell 19, 2300-10.
- Werner, A. et al. (2012) Mol Cell 46, 287-98.
- Zhu, S. et al. (2009) Mol Cell 33, 570-80.
- Swaminathan, S. et al. (2004) J Cell Biol 164, 965-71.
- Takeda, E. et al. (2005) Cell Struct Funct 30, 69-80.
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