Caspase-6 Inhibitor Z-VEID-FMK

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Citations (18)

Caspase-6 Inhibitor Z-VEID-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-6

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
839 (Human); 12368 (Mouse); 83584 (Rat)
Alternate Names
Apoptotic protease Mch-2; CASP6; CASP-6; caspase 6, apoptosis-related cysteine peptidase; caspase 6, apoptosis-related cysteine protease; Caspase6; Caspase-6; EC 3.4.22; Mch2; MCH2EC

Citations for Caspase-6 Inhibitor Z-VEID-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.

18 Citations: Showing 1 - 10
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  1. The caspase-6-p62 axis modulates p62 droplets based autophagy in a dominant-negative manner
    Authors: E Valionyte, Y Yang, SA Griffiths, AT Bone, ER Barrow, V Sharma, B Lu, S Luo
    Cell Death and Differentiation, 2021;0(0):.  2021
  2. Caspase Activation and Caspase-Mediated Cleavage of APP Is Associated with Amyloid beta-Protein-Induced Synapse Loss in Alzheimer's Disease
    Authors: G Park, HS Nhan, SH Tyan, Y Kawakatsu, C Zhang, M Navarro, EH Koo
    Cell Rep, 2020;31(13):107839.  2020
  3. Osteogenic impact of pro-apoptotic caspase inhibitors in MC3T3-E1 cells
    Authors: A Kratochvíl, B Veselá, V Ledvina, E Švandová, K Klepárník, K Dadáková, P Beneš, E Matalová
    Sci Rep, 2020;10(1):7489.  2020
  4. 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
  5. 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
  6. MG132-induced progerin clearance is mediated by autophagy activation and splicing regulation
    Authors: K Harhouri, C Navarro, D Depetris, MG Mattei, X Nissan, P Cau, A De Sandre-, N Lévy
    EMBO Mol Med, 2017;0(0):.  2017
  7. Gene Expression Profiling of Cutaneous Injured and Non-Injured Nociceptors in SNI Animal Model of Neuropathic Pain
    Authors: T Berta, FE Perrin, M Pertin, R Tonello, YC Liu, A Chamessian, AC Kato, RR Ji, I Decosterd
    Sci Rep, 2017;7(1):9367.  2017
  8. Pore-Forming Toxins Induce Macrophage Necroptosis during Acute Bacterial Pneumonia.
    Authors: Gonzalez-Juarbe N, Gilley R, Hinojosa C, Bradley K, Kamei A, Gao G, Dube P, Bergman M, Orihuela C
    PLoS Pathog, 2015;11(12):e1005337.  2015
  9. Disruption of autophagy by the histone deacetylase inhibitor MGCD0103 and its therapeutic implication in B-cell chronic lymphocytic leukemia.
    Authors: El-Khoury V, Pierson S, Szwarcbart E, Brons N, Roland O, Cherrier-De Wilde S, Plawny L, Van Dyck E, Berchem G
    Leukemia, 2014;28(8):1636-46.  2014
  10. Extracellular caspase-6 drives murine inflammatory pain via microglial TNF-alpha secretion.
    Authors: Berta T, Park C, Xu Z, Xie R, Liu T, Lu N, Liu Y, Ji R
    J Clin Invest, 2014;124(3):1173-86.  2014
  11. NAD+ acts on mitochondrial SirT3 to prevent axonal caspase activation and axonal degeneration.
    Authors: Magnifico S, Saias L, Deleglise B, Duplus E, Kilinc D, Miquel M, Viovy J, Brugg B, Peyrin J
    FASEB J, 2013;27(12):4712-22.  2013
  12. Axonal degeneration is regulated by the apoptotic machinery or a NAD+-sensitive pathway in insects and mammals.
    Authors: Schoenmann Z, Assa-Kunik E, Tiomny S, Minis A, Haklai-Topper L, Arama E, Yaron A
    J. Neurosci., 2010;30(18):6375-86.  2010
  13. Superoxide anions and hydrogen peroxide induce hepatocyte death by different mechanisms: involvement of JNK and ERK MAP kinases.
    Authors: Conde de la Rosa L, Schoemaker MH, Vrenken TE, Buist-Homan M, Havinga R, Jansen PL, Moshage H
    J. Hepatol., 2006;44(5):918-29.  2006
  14. Functional proteomics of resveratrol-induced colon cancer cell apoptosis: caspase-6-mediated cleavage of lamin A is a major signaling loop.
    Authors: Lee SC, Chan J, Clement MV, Pervaiz S
    Proteomics, 2006;6(8):2386-94.  2006
  15. Enhancement of stress-induced apoptosis in B-lineage cells by caspase-9 inhibitor.
    Authors: Shah N, Asch RJ, Lysholm AS, Lebien TW
    Blood, 2004;104(9):2873-8.  2004
  16. 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
  17. NuMA and nuclear lamins behave differently in Fas-mediated apoptosis.
    Authors: Taimen P, Kallajoki M
    J. Cell. Sci., 2003;116(0):571-83.  2003
  18. Apaf-1 is a mediator of E2F-1-induced apoptosis.
    Authors: Furukawa Y, Nishimura N, Furukawa Y, Satoh M, Endo H, Iwase S, Yamada H, Matsuda M, Kano Y, Nakamura M
    J. Biol. Chem., 2002;277(42):39760-8.  2002


  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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