SH3BP4 Antibody

SH3BP4 was initially isolated as a novel cDNA using differential display analysis using cultured human corneal fibroblasts. The protein contains three Asn-Pro-Phe (NPF) motifs, an SH3 domain, a PXXP motif, a bipartite nuclear targeting signal, and a tyrosine phosphorylation site. SH3BP4 has been shown to interact with specific endocytic proteins such as clathrin, dynamin, and the transferrin receptor (TfR) and localizes to TfR-containing coated pits and vesicles. It is thought to be involved in cargo-specific control of clathrin-mediated endocytosis, specifically controlling the internalization of TfR. At least two isoforms of SH3BP4 are known to exist.