Render Target: STATIC
Render Timestamp: 2024-12-27T10:44:25.056Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-30 01:53:20.059
Product last modified at: 2024-12-17T18:47:06.204Z
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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-Scribble (Ser1220) (D8A2) Rabbit mAb #12316

Filter:
  • WB

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 240
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    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-Scribble (Ser1220) (D8A2) Rabbit mAb recognizes endogenous levels of scribble protein only when phosphorylated at Ser1220.

    Species Reactivity:

    Human, Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser1220 of human scribble protein.

    Background

    Scribble (Scrib) was originally identified in a genetic screen in Drosophila along with cell polarity determinants Discs Large (Dlg) and Lethal giant larvae (Lgl). Drosophila mutants homozygous for these genes share similar phenotypes, including the loss of apicobasal cell polarity and neoplastic tissue overgrowth. These phenotypic similarities suggest that these three proteins function in a common pathway important for establishing and maintaining apicobasal polarity in epithelial cells (1,2). Scribble contains many leucine-rich repeats and PDZ domains important for localizing scribble to adherens junctions and basolateral regions of mammalian epithelial cells (3). Scribble reportedly binds β-catenin, APC, E-cadherin and the E6 protein from high-risk virus type of HPV through a short motif important for E6-induced cell transformation (4-8). Overexpression of scribble inhibits transformation of rodent epithelial cells by HPV E6/7 proteins (8).
    The phosphorylation state of Scribble has been shown to be functionally important, in part by regulating subcellular localization (9). Mass spectrometry studies have identified phosphorylation at Ser1220 as a frequent modification in a variety of cell and tissue types (10-13). The functional significance of this modification remains to be elucidated.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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