Render Target: STATIC
Render Timestamp: 2024-12-11T11:30:21.030Z
Commit: 611277b6de3cd1bb065350b6ef8d63df412b7185
XML generation date: 2024-08-01 15:29:23.228
Product last modified at: 2024-11-02T14:15:08.539Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Cleaved Gasdermin D (Gly277) Antibody #34667

Filter:
  • WB

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 22
    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

    Cleaved Gasdermin D (Gly277) Antibody recognizes endogenous levels of the carboxy-terminal fragment of gasdermin D protein only when cleaved between Asp276 and Gly277.

    Species Reactivity:

    Mouse

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly277 of mouse gasdermin D protein. Antibodies are purified by peptide affinity chromatography.

    Background

    Gasdermin D (GSDMD), a member of the gasdermin family that includes GSDMA, GSDMB, and GSDMC, has been reported to have a critical role as a downstream effector of pyroptosis (1,2). Pyroptosis is a lytic type of cell death triggered by inflammasomes, multiprotein complexes assembled in response to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) that result in the activation of caspase-1 and subsequent cleavage of pro-inflammatory cytokines IL-1β and IL-18 (3). Gasdermin D was identified by two independent groups as a substrate of inflammatory caspases, caspase-1 and caspase-11/4/5, producing two fragments: GSDMD-N and GSDMD-C. Cleavage results in release of an intramolecular inhibitory interaction between the N- and C-terminal domains, allowing the N-terminal fragment GSDMD-N to initiate pyroptosis through the formation of pores on the plasma membrane (4-7).
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