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Cleaved Caspase-4 (Asp270)/Caspase-5 (Asp327) (F3Q2F) Rabbit Monoclonal Antibody #48139

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  • WB

    Product Specifications

    REACTIVITY H
    SENSITIVITY Transfected Only
    MW (kDa) 36 (casp5), 30 (casp4)
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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

    Cleaved Caspase-4 (Asp270)/Caspase-5 (Asp327) (F3Q2F) Rabbit Monoclonal Antibody recognizes transfected levels of caspase-4 protein only when cleaved between Asp270 and Ser271 and transfected levels of caspase-5 protein only when cleaved between Asp327 and Ser328. This antibody is predicted to detect additional cleavage products of caspase-4 and caspase-5 produced following cleavage of their prodomain sites. This antibody detects a 48 kDa protein of unknown identity in some cell lines.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asp270 of human caspase-4 protein.

    Background

    Canonical activation of the inflammatory necrotic form of cell death, pyroptosis, occurs following inflammasome-mediated activation of caspase-1, leading to cleavage of gasdermin D (1,2). Alternatively, non-canonical cleavage of gasdermin D can be triggered by direct binding of bacterial lipopolysaccharide (LPS) to additional caspases, specifically mouse caspase-11 or human caspase-4 and caspase-5 (2-4). Unlike caspase-4, caspase-5 expression is strongly regulated by inflammatory signals such as LPS and interferon-γ (5). Caspase-4 and caspase-5 activation requires proteolytic processing between three domains: a cascade activation and recruitment domain (CARD), followed by the large and small subunits that form the active protease (6-10). LPS binding to the CARD domain results in cleavage of caspase-4 between the large and small subunits located at Asp270 and Asp289 and at Asp59 in the prodomain (11,12). Equivalent sites are found on caspase-5 at Asp327, Asp346, and Asp137 (13).

    Alternate Names

    apoptotic cysteine protease Mih1/TX; CASP-4; CASP-5; CASP4; CASP5; caspase 4; caspase 4, apoptosis-related cysteine peptidase; caspase 4, apoptosis-related cysteine protease; caspase 5; caspase 5, apoptosis-related cysteine peptidase; caspase 5, apoptosis-related cysteine protease; Caspase-4; Caspase-4 subunit 1; Caspase-4 subunit 2; Caspase-5; Caspase-5 subunit p10; Caspase-5 subunit p20; Caspase4; ICE and Ced-3 homolog 2; ICE(rel)-II; ICE(rel)-III; ICE(rel)II; ICE(rel)III; ICEREL-II; ICEREL-III; ICH-2; ICH-3; ICH2; ICH3; MGC141966; Mih1; Mih1/TX; Protease ICH-2; Protease ICH-3; Protease TX; Protease TY; TX; TY protease

    For Research Use Only. Not for Use in Diagnostic Procedures.
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