Data and information collection on proteins that bind to TAT-CPAP1

ABSTRACT: To elucidate the molecular mechanism by which TAT-CPAP1 acts as a sensitiser, we performed peptide pull-down assays to search for proteins that bind to TAT-CPAP1. We synthesised the biotin-modified peptides Biotin-TAT-CPAP1 and Biotin-TAT-Scramble and conjugated them to streptavidin magnetic beads, and then incubated the bead-peptide complexes with lysates of cisplatin-treated A2780 and OVCAR3 cells, resulting in the final magnetic bead-peptide-binding protein complexes. The binding proteins were then eluted from the magnetic beads, electrophoresed on SDS-PAGE gels and visualised by silver staining. Differential bands present only in the TAT-CPAP1 group were recognised and cut down for mass spectrometry identification (Figure 5A). Only PRDX1 and NPM were uniquely identified in all TAT-CPAP1-treated A2780 and OVCAR3 samples, while being completely absent in all TAT-Scramble-treated controls (Supplemental Table 4). While the most enriched proteins in TAT-CPAP1-treated samples were detected in all groups, proteins exhibited significantly higher levels compared to TAT-Scramble-treated controls.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

DISEASE(S): Malignant Neoplasm Of Ovary

SUBMITTER: zhenlong wang  

LAB HEAD: Xu Juan

PROVIDER: PXD070598 | Pride | 2026-10-26

REPOSITORIES: Pride