Phospho-RCC1 (Ser11) Antibody recognizes endogenous levels of RCC1 protein only when phosphorylated at Ser11.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser11 of human RCC1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
The Ras family small GTPase Ran is involved in nuclear envelope formation, assembly of the mitotic spindle and nuclear transport (1,2). Like other small GTPases, Ran is active in its GTP-bound form and inactive in its GDP-bound form. Nuclear RanGTP concentration is maintained through nuclear localization of guanine nucleotide exchange factor (GEF) activity, which catalyzes the exchange of bound GDP for GTP. RCC1 (regulator of chromatin condensation 1) is the only known RanGEF (3). RCC1 is dynamically chromatin-bound throughout the cell cycle, and this localization is required for mitosis to proceed normally (4,5). Appropriate association of RCC1 with chromatin is regulated through amino-terminal phosphorylation (5,6) and methylation (7). RCC1 regulation of RanGTP levels in response to histone modifications regulates nuclear import during apoptosis (8). In mitosis RCC1 is phosphorylated at Ser11, possibly by cyclinB/cdc2 (9-11). This phosphorylation may play a role in RCC1 interaction with chromatin and its RanGEF activity (6).