Product Pathways - Translational Control
Phospho-PPIG (Ser376) Antibody #3804
|W||H M R Mk||Endogenous||110||Rabbit|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-PPIG (Ser376) Antibody detects endogenous levels of PPIG protein only when phosphorylated at Ser376.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser376 of human PPIG. Antibodies are purified by peptide affinity chromatography.
Western blot analysis of extracts from RL-7 and HEK-293 cells, using Phospho-PPIG (Ser376) Antibody alone (A) or preincubated with either phospho-PPIG (Ser376) peptide (B) or nonphospho-PPIG (Ser376) peptide (C).
PPIG belongs to a highly conserved class of cyclophilins that function as peptidyl-prolyl-isomerases (PPIases) to catalyze the conversion of cis-proline to trans-proline in a polypeptide chain (1-4). PPIG contains an amino-terminal cyclophilin domain followed by Nopp140 repeats that are involved in its function as a nuclear chaperone (5). The carboxy-terminal of PPIG contains a SR (arginine-serine dipeptide repeat) domain (3,4) that is involved in pre-mRNA splicing and processing (6). PPIG interacts with the carboxy-terminal domain of RNA polymerase II as well as several other SR family splicing factors. These interactions lead to changes in localization and conformation and suggest a regulatory role in transcription and pre-mRNA splicing in the elongating RNA polymerase complex (7,8). PPIG is found in the nuclear matrix and nuclear speckles and is involved in the regulation of gene expression. PPIG shows a predominantly diffuse cytoplasmic distribution at the onset of mitosis, and in late telophase the isomerase is recruited to the newly formed nuclei (9).
Phosphorylation of Ser376 on PPIG was identified as a consensus site fit for ACG kinase at Cell Signaling Technology (CST) using PhosphoScan®, a CST's LC-MS/MS platform for phosphorylation site discovery (10).
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- Nestel, F.P. et al. (1996) Gene 180, 151-5.
- Mortillaro, M.J. and Berezney, R. (1998) J Biol Chem 273, 8183-92.
- Meier, U.T. and Blobel, G. (1992) Cell 70, 127-38.
- Zahler, A.M. et al. (1993) Science 260, 219-22.
- Lin, C.L. et al. (2004) Biochem Biophys Res Commun 321, 638-47.
- Bourquin, J.P. et al. (1997) Nucleic Acids Res 25, 2055-61.
- Dubourg, B. et al. (2004) J Biol Chem 279, 22322-30.
- Rush, J. et al. (2005) Nat Biotechnol 23, 94-101.
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For Research Use Only. Not For Use In Diagnostic Procedures.