|Tested applications||WB IHC FC|
|Recommended Dilution||WB 1:100 - 1:500
IHC 1:50 - 1:100
FC 1:20 - 1:50|
|Observed MW||Refer to Figures|
|Immunogen||A synthetic peptide of human PPIG|
|Storage Buffer||Store at 4℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
|Synonym||PPIG; Peptidyl-prolyl cis-trans isomerase G; CASP10; Clk-associating RS-cyclophilin; Cyclophilin G; Rotamase G;|
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).
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