| Products/Services Used | Details | Operation |
|---|---|---|
| Peptide Synthesis | Anti-cavin-1 (PTRF) pAb (cat #18892-1) and Anti-cavin-2 (SDPR) pAb (cat #12339-1) were from ProteinTech group (Chicago, IL). Chicken polyclonal β-galactosidase antibody (cat #ab9361) was from Abcam. Rabbit polyclonal von Willebrand Factor antibody (cat #AB7356) obtained from Millipore Corp. Rabbit polyclonal antibody against EphB1 sequence (AA 528-541, DDDYKSELREQLPL) (anti-EphB1 pAb) was custom produced by Sigma-Aldrich (St. Louis, MO). Anti-EphB1 mouse monoclonal against EphB1 sequence (AA 528-541, DDDYKSELREQLPL) was custom made by GenScript. N-terminal biotin labeled cell permeable antennapedia peptide (AP; RQIKIWFQNRRMKWKK); Cav-1 scaffold domain peptide (DGIWKASFTTFTVTKYWFYR) as a fusion peptide to the C terminus of the N-terminal biotin labeled AP; and EphB1 panning (receptor antagonistic) peptide (EWLSPNLAPSVRGSGSK) and scrambled control peptide (RTVAHHGGLYHTNAEVK) were synthesized by GenScript. | Get A Quote |
Caveolae, the cave-like structures abundant in endothelial cells (ECs), are important in regulating key functions such as caveolae-mediated endocytosis and generation of nitric oxide. Here we show that deletion of the receptor tyrosine kinase EphB1 (EphB1−/−) in mice markedly reduced the caveolae number in ECs of heart and lung vessels and prevented caveolae-mediated endocytosis. EphB1 expressed in adult ECs was shown to bind the caveolin-1 (Cav-1) scaffold domain (CSD) via the CSD binding motif (CSDBM) on EphB1. We demonstrated that activation of EphB1 by the native ligand Ephrin B1 uncoupled EphB1 from Cav-1, and licensed Src-dependent Y-14 Cav-1 phosphorylation. Deletion of CSDBM on EphB1 prevented EphB... More
