Render Target: SSR
Render Timestamp: 2024-12-03T20:20:37.625Z
Commit: cd2fae6ca3f811b1ddb1df24ac291ed56d5d501b
XML generation date: 2021-12-31 18:48:12.890
Product last modified at: 2024-05-30T07:15:27.479Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Cleaved Gasdermin D (Asp276) Antibody (Mouse Specific) #50928

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  • WB

Inquiry Info. # 50928

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    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 31
    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 (Asp276) Antibody (Mouse Specific) recognizes endogenous levels of amino-terminal fragment of Gasdermin D protein only when cleaved at Asp276.

    Species Reactivity:

    Mouse

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp276 of mouse Gasdermin D protein. Antibodies are purified by protein A and 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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