Z-VAD-FMK (Cell permeable) - Order from Adipogen

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Product Data
Synonyms	Z-VAD(OMe)-FMK; pan-Caspase Inhibitor; Z-Val-Ala-DL-Asp(OMe)-fluoromethylketone; Benzyloxycarbonyl-Val-Ala-DL-Asp(OMe)-fluoromethylketone
Properties
Formula	C₂₂H₃₀FN₃O₇
MW	467.5
CAS	187389-52-2 and 634911-81-2
Source/Host Chemicals	Synthetic.
Purity	≥95% (HPLC)
Appearance	White solid.
Solubility	Soluble in DMSO, acetonitrile or dimethyl formamide.
Other Product Data	Prepare a 10mM stock solution of the caspase inhibitor in high quality DMSO. Add 2μl of stock solution to 1ml of culture medium containing cells to give 20μM final concentration. Effective final concentrations are estimated to be 5-20μM. If a particular inhibitor is applied at higher concentrations, specificity for an individual caspase or even for the caspase family (>100μM) might be compromised. DMSO concentrations above 0.2% may cause cellular toxicity, thus masking the effect of the caspase inhibitor. For in vivo experiments extending 12 to 48 hours, fresh inhibitor may have to be added (injected) due to inactivation by reaction with cysteine protease.
InChi Key	MIFGOLAMNLSLGH-SXUUOERCBK
Product Type	Chemical
Shipping and Handling
Shipping	AMBIENT
Short Term Storage	+4°C
Long Term Storage	-20°C
Handling Advice	Keep cool and dry.
Use/Stability	Stable for at least 3 years after receipt when stored at -20°C.
Documents
MSDS	Download

Product Description

Cell permeable, non-selective broad-spectrum caspase inhibitor [1, 3, 7, 8]. Binds irreversibly to the catalytic site of caspase proteases [1].
The peptide is O-methylated in the P1 position on aspartic acid, providing enhanced stability and increased cell permeability [1].
Inhibits ICE-family protease/caspase processing, leading to apoptosis and autophagy induction [2-4, 6, 9].
Decreases proteasome activity [5].
Potent inhibitor of caspase-1 activation in NLRP3/NALP3-induced cells [11].
Used in apoptosis and inflammasome studies.

Product References

Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32: E.A. Slee, et al.; Biochem. J. 315, 21 (1996) Different interleukin-1 beta converting enzyme (ICE) family protease requirements for the apoptotic death of T lymphocytes triggered by diverse stimuli: A. Sarin, et al.; J. Exp. Med. 184, 2445 (1996) Processing/activation of at least four interleukin-1beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells: M. MacFarlane, et al.; J. Cell Biol. 137, 469 (1997) Processing/activation of caspases, -3 and -7 and -8 but not caspase-2, in the induction of apoptosis in B-chronic lymphocytic leukemia cells: D. King, et al.; Leukemia 12, 1553 (1998) Proteasome activities decrease during dexamethasone-induced apoptosis of thymocytes: J. Beyette, et al.; Biochem. J. 332, 315 (1998) JNK (c-Jun N-terminal kinase) and p38 activation in receptor-mediated and chemically-induced apoptosis of T-cells: differential requirements for caspase activation: M. MacFarlane, et al.; Biochem. J. 348, 93 (2000) Statin-induced proinflammatory response in mitogen-activated peripheral blood mononuclear cells through the activation of caspase-1 and IL-18 secretion in monocytes: W.R. Coward, et al.; J. Immunol. 176, 5284 (2006) Broad-spectrum caspase inhibitors: from myth to reality? D. Chauvier, et al.; Cell Death Differ. 14, 387 (2007) A calpain-like protease inhibits autophagic cell death: D.T. Madden, et al.; Autophagy 3, 519 (2007) Malarial hemozoin is a Nalp3 inflammasome activating danger signal; C. Dostert, et al.; PLoS One 4, e6510 (2009)

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