Caspase-10 Inhibitor Z-AEVD-FMK

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Citations (10)

Caspase-10 Inhibitor Z-AEVD-FMK Summary

Cell permeable fluoromethyl ketone (FMK)-derivatized peptides act as effective irreversible Caspase inhibitors with no cytotoxic effects and, therefore, are useful tools for studying Caspase activity.


Shipping Conditions
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.

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Background: Caspase-10

Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. They are expressed as latent zymogens and are activated by an autoproteolytic mechanism or by processing by other proteases (frequently other caspases). Human caspases can be subdivided into three functional groups: cytokine activation (caspase-1, -4, -5, and -13), apoptosis initiation (caspase-2, -8, -9, -and -10), and apoptosis execution (caspase-3, -6, and -7).

Caspases are regulated by a variety of stimili, including APAF1, CFLAR/FLIP, NOL3/ARC, and members of the inhibitor of apoptosis (IAP) family such as BIRC1/NAIP, BIRC2/cIAP-1, BIRC3/cIAP-2, BIRC4/XIAP, BIRC5/Survivin, and BIRC7/Livin. IAP activity is modulated by DIABLO/SMAC or PRSS25/HTRA2/Omi. Cell-permeable and irreversible peptide inhibitors are also available for different caspases.

Entrez Gene IDs
843 (Human)
Alternate Names
Apoptotic protease Mch-4; CASP10; CASP-10; caspase 10, apoptosis-related cysteine peptidase; caspase 10, apoptosis-related cysteine protease; Caspase10; Caspase-10; EC; FADD-like ICE2; FAS-associated death domain protein interleukin-1B-converting enzyme 2; FLICE2; ICE-like apoptotic protease 4; interleukin-1B-converting enzyme 2; Mch4; MCH4ALPS2

Citations for Caspase-10 Inhibitor Z-AEVD-FMK

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

10 Citations: Showing 1 - 10
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  1. TRAF3/p38-JNK Signalling Crosstalk with Intracellular-TRAIL/Caspase-10-Induced Apoptosis Accelerates ROS-Driven Cancer Cell-Specific Death by CD40
    Authors: K Ibraheem, AMA Yhmed, MM Nasef, NT Georgopoul
    Cells, 2022;11(20):.  2022
  2. The mechanism of how CD95/Fas activates the Type I IFN/STAT1 axis, driving cancer stemness in breast cancer
    Authors: AS Qadir, AM Stults, AE Murmann, ME Peter
    Sci Rep, 2020;10(1):1310.  2020
  3. Bacterial Pore-Forming Toxins Promote the Activation of Caspases in Parallel to Necroptosis to Enhance Alarmin Release and Inflammation During Pneumonia
    Authors: N Gonzalez-J, KM Bradley, AN Riegler, LF Reyes, T Brissac, SS Park, MI Restrepo, CJ Orihuela
    Sci Rep, 2018;8(1):5846.  2018
  4. Synergistic Antitumour Properties of viscumTT in Alveolar Rhabdomyosarcoma
    Authors: RM Stammer, S Kleinsimon, J Rolff, S Jäger, A Eggert, G Seifert, CI Delebinski
    J Immunol Res, 2017;2017(0):4874280.  2017
  5. Lipopolysaccharide (LPS) Promotes Apoptosis in Human Breast Epithelial x Breast Cancer Hybrids, but Not in Parental Cells.
    Authors: Fried S, Tosun S, Troost G, Keil S, Zaenker K, Dittmar T
    PLoS ONE, 2016;11(2):e0148438.  2016
  6. Inhibition of cancer cell proliferation and apoptosis-inducing activity of fungal taxol and its precursor baccatin III purified from endophytic Fusarium solani.
    Authors: Chakravarthi B, Sujay R, Kuriakose G, Karande A, Jayabaskaran C
    Cancer Cell Int, 2013;13(1):105.  2013
  7. Zoledronic acid significantly enhances radiationinduced apoptosis against human fibrosarcoma cells by inhibiting radioadaptive signaling.
    Authors: Koto K, Murata H, Kimura S, Sawai Y, Horie N, Matsui T, Ryu K, Ashihara E, Maekawa T, Kubo T, Fushiki S
    Int J Oncol, 2013;42(2):525-34.  2013
  8. Brahma is essential for Drosophila intestinal stem cell proliferation and regulated by Hippo signaling.
    Authors: Jin, Yunyun, Xu, Jinjin, Yin, Meng-Xin, Lu, Yi, Hu, Lianxin, Li, Peixue, Zhang, Peng, Yuan, Zengqian, Ho, Margaret, Ji, Hongbin, Zhao, Yun, Zhang, Lei
    Elife, 2013;2(0):e00999.  2013
  9. HIV-1 tat protein and cell proliferation and survival: a brief review.
    Authors: Gibellini D, Vitone F, Schiavone P, Re MC
    New Microbiol., 2005;28(2):95-109.  2005
  10. Increased sensitivity of early apoptotic cells to complement-mediated lysis.
    Authors: Attali G, Gancz D, Fishelson Z
    Eur. J. Immunol., 2004;34(11):3236-45.  2004


  1. Does R&D Systems offer a negative control for Caspase Inihibitors with benzyloxycarbonyl group (Z-) at the N-terminus and the FMK functional group at the C-terminus?

    • Yes, R&D Systems offers Caspase Inhibitor Control Z-FA-FMK, Catalog # FMKC01, which is an inhibitor of cathepsins B and L but not caspases, and has been used in several systems as a negative control for peptide inhibitors of caspases.

  2. Are R&D Systems Caspase Inhibitors irreversible?

    • Yes, the majority of R&D Systems Caspase Inhibitors have a Fluoromethyl ketone (FMK) functional group on the C-terminus of the peptide, and act as effective irreversible inhibitors with no added cytotoxic effects. Inhibitors synthesized with a benzyloxycarbonyl group (also known as BOC or Z) at the N-terminus and O-methyl side chains exhibit enhanced cellular permeability.

      R&D Systems also offers a General Caspase Inhibitor, Q-VD-OPh, Catalog # OPH001, as well as a FITC-conjugated pan-caspase inhibitor (ApoStat), Catalog # FMK012, which are both cell-permeable, irreversible inhibitors of caspase activity.

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