1. Recombinant Proteins
  2. Enzymes & Regulators
  3. Caspase
Cat. No. Product Name / Synonyms Species Source
  • HY-P74347
    Caspase-7/CASP7 Protein, Human (His)

    CMH-1; CASP-7; Caspase-7; MCH3; ICE-LAP3

    Human E. coli
    Caspase-7/CASP7 protein is a thiol protease involved in programmed cell death processes such as apoptosis, pyroptosis, and granzyme-mediated death. It is activated by initiating caspases (CASP8, CASP9 and/or CASP10) and cleaves CLSPN, PARP1, PTGES3 and YY1, mediating apoptosis. Caspase-7/CASP7 Protein, Human (His) is the recombinant human-derived Caspase-7/CASP7 protein, expressed by E. coli , with C-His labeled tag. The total length of Caspase-7/CASP7 Protein, Human (His) is 303 a.a., with molecular weight of ~20 & 11 kDa, respectively.
  • HY-P71708
    Caspase-8/CASP8 subunit p18 Protein, Human (His)

    ALPS2B; CASP-8; ICE-like apoptotic protease 5

    Human E. coli
    The Caspase-8/CASP8 subunit p18 protein is a key thiol protease that acts as a molecular switch in programmed cell death processes, including apoptosis, necroptosis, and pyroptosis. It is essential for preventing tissue damage by inducing exogenous apoptosis by cleaving and activating effector caspases. Caspase-8/CASP8 subunit p18 Protein, Human (His) is the recombinant human-derived Caspase-8/CASP8 subunit p18 protein, expressed by E. coli , with N-6*His labeled tag. The total length of Caspase-8/CASP8 subunit p18 Protein, Human (His) is 158 a.a., with molecular weight of ~21.9 kDa.
  • HY-P72117
    Caspase-1/CASP1 Protein, Human (GST)

    CASP-1; CASP1; CASP1_HUMAN; Caspase 1; 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

    Human E. coli
    Caspase-1/CASP1 is a thiol protease complex involved in inflammation by catalyzing the cleavage of IL1B, IL18, and Gasdermin-D (GSDMD). It activates a pro-inflammatory response, releases mature cytokines IL1B and IL18, and initiates pyroptosis through cleavage of GSDMD. Caspase-1/CASP1 Protein, Human (GST) is the recombinant human-derived Caspase-1/CASP1 protein, expressed by E. coli , with N-GST labeled tag. The total length of Caspase-1/CASP1 Protein, Human (GST) is 150 a.a., with molecular weight of ~43.8 kDa.
  • HY-P7743
    Caspase-14/CASP14 Protein, Human (His)

    rHuCaspase-14, His; Caspase-14; CASP-14; CASP14

    Human E. coli
    Caspase-14 Protein, Human (His) is an approximately 31.0 kDa caspase-14 protein with a His-flag. Caspase-14 is a seemingly non-apoptotic caspase involved in keratinocyte differentiation and cornification.
  • HY-P701341
    Caspase-3/CASP3 Protein, Human

    CASP3; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1

    Human E. coli
    Caspase-3/CASP3 protein is a thiol protease critical in apoptosis and is activated by initiating caspases (CASP8, CASP9 and/or CASP10). It catalyzes the cleavage of multiple proteins in sympathetic neurons, including PARP1, SREBP, caspase-6, -7 and -9, huntingtin, and RET. Caspase-3/CASP3 Protein, Human is the recombinant human-derived Caspase-3/CASP3 protein, expressed by E. coli , with tag free. The total length of Caspase-3/CASP3 Protein, Human is 277 a.a., .
  • HY-P7742
    Caspase-10/CASP10 Protein, Human (His)

    rHuCaspase-10, His; Caspase-10; CASP-10; Apoptotic Protease Mch-4; ICE-Like Apoptotic Protease 4; CASP10; MCH4

    Human E. coli
    Caspase-10 Protein, Human (His) is an approximately 33.0 kDa caspase-10 protein with a His-flag, expressed in E. coli. Caspase-10 belongs to the caspase family and involved in the execution-phase of cell apoptosis.
  • HY-P701342
    Caspase-3/CASP3 Protein, Human (His, Strep)

    CASP3; Caspase-3; CASP-3; Apopain; Cysteine protease CPP32; CPP-32; Protein Yama; SREBP cleavage activity 1; SCA-1

    Human E. coli
    Caspase-3/CASP3 protein is a thiol protease critical in apoptosis and is activated by initiating caspases (CASP8, CASP9 and/or CASP10). It catalyzes the cleavage of multiple proteins in sympathetic neurons, including PARP1, SREBP, caspase-6, -7 and -9, huntingtin, and RET. Caspase-3/CASP3 Protein, Human (His, Strep) is the recombinant human-derived Caspase-3/CASP3 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of Caspase-3/CASP3 Protein, Human (His, Strep) is 277 a.a., .
Cat. No. Product Name Effect Purity

Upon binding to their cognate ligand, death receptors such as Fas and TRAILR can activate initiator Caspases (Pro-caspase 8 and Pro-caspase 10) through dimerization mediated by adaptor proteins such as FADD and TRADD. Active Caspase 8 and Caspase 10 then cleave and activate the effector Caspase 3, 6 and 7, leading to apoptosis. ROS/DNA damage and ER stress trigger Caspase 2 activation. Active Caspase 2 cleaves and activates Caspase 3 and initiates apoptosis directly. Caspase 2, 8 and 10 can also cleave Bid, stimulate mitochondrial outer membrane permeabilization (MOMP) and initiate the intrinsic apoptotic pathway. Following MOMP, mitochondrial intermembrane space proteins such as Smac and Cytochrome C are released into the cytosol. Cytochrome C interacts with Apaf-1, triggering apoptosome assembly, which activates Caspase 9. Active Caspase 9, in turn, activates Caspase 3, 6 and 7, leading to apoptosis. Mitochondrial release of Smac facilitates apoptosis by blocking the inhibitor of apoptosis (IAP) proteins. 

 

Following the binding of TNF to TNFR1, TNFR1 binds to TRADD, which recruits RIPK1, TRAF2/5 and cIAP1/2 to form TNFR1 signaling complex I. Formation of the complex IIa and complex IIb is initiated either by RIPK1 deubiquitylation mediated by CYLD or by RIPK1 non-ubiquitylation due to depletion of cIAPs. The Pro-caspase 8 homodimer in complex IIa and complex IIb generates active Caspase 8. This active Caspase 8 in the cytosol then carries out cleavage reactions to activate downstream executioner caspases and thus induce classical apoptosis[1][2]

 

Reference:

[1]. Thomas C, et al. Caspases in retinal ganglion cell death and axon regeneration. Cell Death Discovery volume 3, Article number: 17032 (2017).
[2]. Brenner D, et al. Regulation of tumour necrosis factor signalling: live or let die. Nat Rev Immunol. 2015 Jun;15(6):362-74.