Render Target: STATIC
Render Timestamp: 2025-01-09T11:30:41.639Z
Commit: 199712eb9daea12d88cc0e67894a8a09f475f8cb
XML generation date: 2024-08-01 15:28:48.820
Product last modified at: 2024-05-30T07:16:50.327Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-RIP3 (Thr231/Ser232) Antibody (Mouse Specific) #57220

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    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 46-62
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • 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 and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-RIP3 (Thr231/Ser232) Antibody (Mouse Specific) recognizes endogenous levels of RIP3 protein only when phosphorylated at Thr231/Ser232. This antibody may not react with single phosphorylation at either site.

    Species Reactivity:

    Mouse

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Thr231/Ser232 of mouse RIP3 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8).
    Receptor-interacting protein 3 (RIP3) was originally found to interact with RIP and the TNF receptor complex to induce apoptosis and activation of NF-κB (9,10). It has subsequently been shown that the association between RIP and RIP3 is a key component of a signaling pathway that results in programmed necrosis (necroptosis), a necrotic-like cell death induced by TNF in the presence of caspase inhibitors (11-13). RIP3 is phosphorylated at Ser227 and targets the phosphorylation of mixed lineage kinase domain-like protein (MLKL), which is critical for necroptosis (14). In mice, RIP3 is phosphorylated at Thr231 and Ser232, leading to association with MLKL and necroptosis (15).
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