PPIL1 Antibody (LB-72): sc-100701

PPIL1 Antibody (LB-72) is a mouse monoclonal IgG2a kappa light chain antibody that detects PPIL1 in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-PPIL1 antibody (LB-72) is offered as a non-conjugated format. PPIL1, also known as peptidylprolyl isomerase (cyclophilin)-like 1, CYPL1, PPIase, CGI-124, or hCyPX, is a crucial member of the cyclophilin-type peptidylprolyl isomerase family, characterized by a single PPIase cyclophilin-type domain. PPIL1 is ubiquitously expressed, with particularly high levels found in skeletal muscle and heart tissues, highlighting PPIL1′s importance in muscle function and cardiac health. PPIL1 plays a significant role in spliceosome assembly, as PPIL1 is a component of the 35 S U5 small nuclear ribonucleoprotein and is recruited to the 45 S activated spliceosome by Skip (SNW1), a transcriptional coactivator. This interaction suggests PPIL1 may function as a molecular chaperone or foldase, facilitating proper assembly and activation of the spliceosome, which is essential for pre-mRNA splicing. PPIL1 has been shown to interact with Op18, a protein that stabilizes microtubules, indicating PPIL1′s potential involvement in cell proliferation and cytoskeleton regulation. Elevated expression levels of PPIL1 in cancer cells underscore PPIL1′s role in proliferation and tumorigenesis, making PPIL1 a significant target for cancer biology research.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

PPIL1 Antibody (LB-72) References:

1. Reassignment of peptidyl prolyl isomerase-like 1 gene (PPIL1) to human chromosome region 6p21.1 by radiation hybrid mapping and fluorescence in situ hybridization.  |  Mann, SS., et al. 1998. Cytogenet Cell Genet. 83: 228-9. PMID: 10072585
2. Cyclophilins of a novel subfamily interact with SNW/SKIP coregulator in Dictyostelium discoideum and Schizosaccharomyces pombe.  |  Skruzný, M., et al. 2001. Biochim Biophys Acta. 1521: 146-51. PMID: 11690648
3. Transcriptional coregulator SNW/SKIP: the concealed tie of dissimilar pathways.  |  Folk, P., et al. 2004. Cell Mol Life Sci. 61: 629-40. PMID: 15052407
4. Overexpression of peptidyl-prolyl isomerase-like 1 is associated with the growth of colon cancer cells.  |  Obama, K., et al. 2006. Clin Cancer Res. 12: 70-6. PMID: 16397026
5. Solution structure of human peptidyl prolyl isomerase-like protein 1 and insights into its interaction with SKIP.  |  Xu, C., et al. 2006. J Biol Chem. 281: 15900-8. PMID: 16595688
6. Cloning, expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain.  |  Ozaki, K., et al. 1996. Cytogenet Cell Genet. 72: 242-5. PMID: 8978786