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Recombinant Human Caspase-1 (CASP1), Truncated

ACP24715

Number
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Main Attributes


Cat.No ACP24715 Target NameCASP1
FormLiquid or Lyophilized powderExpression SystemE.coli
Expression Range120-269aaMol Weight43.8kDa
Protein LengthPartialPurityGreater than 90% as determined by SDS-PAGE.
Storage Buffer5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0.

Others Attributes


Target SpeciesHumanUniprot IDP29466
Background Information
  • Uniprot Id

    P29466

  • Target Species

    Human

  • Target Name

    CASP1

  • Target Full Name

    Caspase-1

  • Target Function

    Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a proinflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukins IL1B and IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly.; Apoptosis inactive.; Apoptosis inactive.

  • Target Subcellular Location

    Cytoplasm. Cell membrane.

  • Target Protein Families

    Peptidase C14A family

  • Target Tissue Specificity

    Expressed in larger amounts in spleen and lung. Detected in liver, heart, small intestine, colon, thymus, prostate, skeletal muscle, peripheral blood leukocytes, kidney and testis. No expression in the brain.

  • Target Research Area

    Apoptosis

  • Target Synonyms

    CASP-1; CASP1; CASP1_HUMAN; Caspase 1; Caspase-1 subunit p10; ICE; IL-1 beta-converting enzyme; IL-1BC; IL1 beta converting enzyme; IL1B convertase; Interleukin 1 beta convertase; Interleukin 1B converting enzyme; Interleukin-1 beta convertase; Interleukin-1 beta-converting enzyme; p45

  • Target Background

    This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing results in transcript variants encoding distinct isoforms.

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