Render Target: STATIC
Render Timestamp: 2024-11-21T13:34:05.647Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:28:50.918
Product last modified at: 2024-10-24T10:30:45.286Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Gasdermin E Antibody #40618

Filter:
  • WB

    Supporting Data

    REACTIVITY M R
    SENSITIVITY Endogenous
    MW (kDa) 57, 33
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • M-Mouse 
    • R-Rat 

    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

    Gasdermin E Antibody recognizes endogenous levels of total Gasdermin E protein. This antibody can also detect the amino-terminal cleavage fragment associated with pyroptosis.

    Species Reactivity:

    Mouse, Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding His112 of mouse Gasdermin E protein. Antibodies are purified by peptide affinity chromatography.

    Background

    The gasdermin family, which includes GSDMA, GSDMB, GSDMC, GSDMD, and GSDME, has been shown to play a role in inflammation and cell death. Gasdermin D 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).

    Gasdermin E (GSDME), also known as DFNA5, was originally identified as a genetic cause of nonsyndromic hearing loss (8). Like other gasdermin family members, Gasdermin E contains an amino-terminal pore forming domain that triggers pyroptosis. Cleavage of Gasdermin E at Asp270 is induced by apoptotic-associated Caspase-3, converting apoptotic signals to pyroptosis (9). In addition, cleavage of Gasdermin E can be induced by Granzyme B secreted by NK cells and contributes to tumor suppressive activity (10). Gasdermin E expression is suppressed in several types of cancer including gastric, colorectal, and breast carcinoma, and may be associated with decreased survival (11-13). In contrast, an increase in Gasdermin E, including the amino-terminal pore-forming fragment, is associated with conditions of excessive inflammation (14-16).
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