PPIG antibody Usage And Synthesis

Source

Rabbit

Reactivity

Human;Mouse;Rat

Background

PPIG belongs to a highly conserved class of cyclophilins that function as peptidyl-prolyl-isomerases to catalyze the conversion of cis-proline to trans-proline in a polypeptide chain. PPIG contains an amino-terminal cyclophilin domain followed by Nopp140 repeats that are involved in its function as a nuclear chaperone. The carboxy-terminal of PPIG contains a SR domain that is involved in pre-mRNA splicing and processing. 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. 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.

References

[1] Fischer, G. et al. (1989) Nature 337, 476-8.
[2] Freskgård, P.O. et al. (1992) Science 258, 466-8.
[3] Nestel, F.P. et al. (1996) Gene 180, 151-5.
[4] Mortillaro, M.J. and Berezney, R. (1998) J Biol Chem 273, 8183-92.
[5] Meier, U.T. and Blobel, G. (1992) Cell 70, 127-38.
[6] Zahler, A.M. et al. (1993) Science 260, 219-22.
[7] Lin, C.L. et al. (2004) Biochem Biophys Res Commun 321, 638-47.
[8] Bourquin, J.P. et al. (1997) Nucleic Acids Res 25, 2055-61.
[9] Dubourg, B. et al. (2004) J Biol Chem 279, 22322-30.

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