REPS1 (RalBP1-associated Eps Domain-containing Protein 1, RalBP1-interacting Protein 1)

REPS1 is a RalBP1-associated EH-homology domain containing protein. The sequence of REPS1 has a 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 also have been shown to interact with the SH3 domain of intersectin1 (ITSN1) and contribute to ITSN1/SGIP1/REPS1 complex formation on clathrin-coated pits. Three alternatively spliced isoforms have been identified.\n\nApplications: \nSuitable for use in Western Blot and Immunoprecipitation. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: 1:1000\nImmunoprecipitation: 1:50\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

R1035-74A

Size

100ul

Applications

IP, WB

Hosts

Rabbit

Reactivities

Hum

Form

Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.

P Type

Pab

Purity

Purified by Protein A affinity chromatography.

Isotype

IgG

References

1.Yamaguchi, A. et al. (1997) J Biol Chem 272, 31230-4. 2.Cullis, D.N. et al. (2002) J Biol Chem 277, 49158-66. 3.Dergai, O. et al. (2010) Biochem Biophys Res Commun 402, 408-13.

Additional Info

Recognizes endogenous levels of total human REPS1.