Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Phospho-REPS1 (Ser709) Antibody recognizes endogenous levels of REPS1 only when phosphorylated at Ser709.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser709 of human REPS1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
REPS1 is a RalBP1-associated EH-homology domain containing protein. The sequence of REPS1 has an EH domain, followed by two proline-rich segments, and a C-terminal coiled-coil domain for binding to RalBP1 (1). The EH domain of REPS1 interacts with the NPF motif of Rab11-FIP2, mediates their colocalization to endosome vesicles, and influences EGFR endocytosis (2). The two proline-rich regions of REPS1 are important for binding to the SH3 domain of GRK/GRB2 and further regulate EGFR downstream signaling. The proline-rich regions of REPS1 have also been shown to interact with the SH3 domain of intersectin1 (ITSN1) and contribute to ITSN1/SGIP1/REPS1 complex formation on clathrin-coated pits (3). Three alternatively spliced isoforms of REPS1 have been identified.
Phosphorylation of Ser709 on REPS1 was identified at Cell Signaling Technology using PTMScan® Technology, our LC-MS/MS platform for phosphorylation site discovery (4).
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
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