Render Target: STATIC
Render Timestamp:
3/26/2025, 10:42:45 AM EDT
3/26/2025, 2:42:45 PM UTC
Commit: 461ca8d8fe5b1efd4c01fc87e5b5eb592e2d154a
XML generation date: 2025-03-07 13:06:17.419
Product last modified at: 2025-02-11T00:30:09.496Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-REPS1 (Ser709) (D8C1) Rabbit mAb #12005

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H Mk
    SENSITIVITY Endogenous
    MW (kDa) 125
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-REPS1 (Ser709) (D8C1) Rabbit mAb recognizes endogenous levels of REPS1 protein only when phosphorylated at Ser709.

    Species Reactivity:

    Human, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser709 of human REPS1 protein.

    Background

    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 REPS1 at Ser709 was identified at Cell Signaling Technology using PTMScan® Technology, our LC-MS/MS platform for phosphorylation site discovery (4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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