Memo (N-terminal region) Antibody

During cell migration, actin assembly drives cell membrane protrusion, while microtubules (MTs) extend within protrusions to promote adhesion site turnover. Memo (mediator of ErbB2-driven cell motility) is an effector of the ErbB2 receptor tyrosine kinase involved in breast carcinoma cell migration. This effector may be important for mediating ErbB2-regulated changes in actin and MT dynamics during cell motility. Memo, a 297-amino-acid protein, has homology to class III nonheme iron-dependent dioxygenases, however it has not been shown to display metal binding or enzymatic activity. It has been shown to bind ErbB2 (Tyr-1227) phosphopeptide via its putative enzymatic active site. Memo and PLCγ1 interaction with ErbB2 is essential for HRG-induced chemotaxis. Furthermore, organization of the lamellipodial actin network is coordinated by signaling from Memo to the RhoA–mDia1 pathway localized to the plasma membrane. In addition, Memo may regulate actin dynamics by promoting cofilin depolymerizing and severing of F-actin

Memo synthetic peptide (coupled to KLH) corresponding to amino acid residues in the N-terminal region of human Memo. This peptide sequence is highly conserved in rat, mouse, and chicken Memo.

The antibody detects a significant 33 kDa* protein corresponding to the molecular mass of Memo on SDS-PAGE immunoblots of mouse heart, mouse C2C12, and rabbit spleen fibroblasts.