Overview

Description

  • NatureSynthetic
  • SourceCHO
  • Amino Acid Sequence
    • AccessionP42574
    • SpeciesHuman

Specifications

Our Abpromise guarantee covers the use of ab13848 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Blocking - Blocking peptide for Anti-active + pro Caspase 3 antibody (ab13847), Anti-active Caspase-3 antibody (ab77973)

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Information available upon request.

General info

  • Alternative names
    • APOPAIN
    • Apopain precursor
    • Apopain precursor
    • CASP 3
    • CASP-3
    • CASP3
    • CASP3
    • CASP3_HUMAN
    • Caspase 3
    • Caspase 3 apoptosis related cysteine protease
    • Caspase 3 apoptosis related cysteine protease
    • Caspase-3 subunit p12
    • Caspase3
    • CPP 32
    • CPP 32
    • CPP-32
    • CPP32
    • CPP32B
    • CPP32B
    • Cysteine protease CPP32
    • Cysteine protease CPP32
    • Human cysteine protease CPP32 isoform alpha mRNA complete cds
    • Human cysteine protease CPP32 isoform alpha mRNA complete cds
    • ICE3
    • ICE3
    • LICE
    • LICE
    • PARP cleavage protease
    • PARP cleavage protease
    • Protein Yama
    • SCA 1
    • SCA-1
    • SCA1
    • SREBP cleavage activity 1
    • SREBP cleavage activity 1
    • Yama
    • Yama protein
    • Yama protein
    see all
  • FunctionInvolved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-
    -Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.
  • Tissue specificityHighly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.
  • Sequence similaritiesBelongs to the peptidase C14A family.
  • Post-translational
    modifications
    Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.
    S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.
  • Cellular localizationCytoplasm.
  • Information by UniProt

References for Human active Caspase-3 peptide (ab13848)

ab13848 has not yet been referenced specifically in any publications.

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