Anti-SH3 domain-binding protein 4 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.

SH3BP4 antibody was raised against an 18 amino acid synthetic peptide from near the carboxy terminus of human SH3BP4. The immunogen is located within amino acids 860 - 910 of SH3BP4.

May function in transferrin receptor internalization at the plasma membrane through a cargo-specific control of clathrin- mediated endocytosis. Alternatively, may act as a negative regulator of the amino acid-induced TOR signaling by inhibiting the formation of active Rag GTPase complexes. Preferentially binds inactive Rag GTPase complexes and prevents their interaction with the mTORC1 complex inhibiting its relocalization to lysosomes and its activation. Thereby, may indirectly regulate cell growth, proliferation and autophagy.

SH3BP4 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle. Nucleus . Specifically associated with transferrin receptor-containing clathrin-coated pits and clathrin-coated vesicles. May also localize to the nucleus.