Caspase-8 Inhibitor Z-IETD-FMK for cell activation

Catalog number
1064-100
Name
Caspase-8 Inhibitor Z-IETD-FMK for cell activation
Size
100 µl (2 mM)
Price
186.00 EUR
Supplier

Details

Description
A synthetic peptide that irreversibly inhibits FLICE and related protease/caspase activity and blocks apoptosis. IETD is the specific recognition sequence found in CPP32 proenzyme. The inhibitor is designed as a methyl ester to facilitate cell permeability. (CAUTION: If the intended use is on purified or recombinant enzymes, esterase should be added to generate free carboxyl groups.)
Peptide sequence
Z-Ile-Glu(OMe)-Thr-Asp(OMe)-FMK
CAS number
N/A
Molecular weight
654.7
Category
Caspase Substrate
Other name
Z-IETD-FMK, Caspase-8 Inhibitor, Z-IETD-fluoromethylketone
Molecular formula
C₃₀H₄₃FN₄O₁₁
Physical appearance
Liquid
Supplied with
DMSO (2 mM)
Is this a salt?
No
Is it cell-permeable?
Yes
Purification
>99% by HPLC
Reconstitute instructions
N/A
Storage condition
-20°C
Shipping condition
gel pack
Maximum time for storage
12 months
Storage instructions
Protect from light and moisture
Tissue
cell
Additional description
Human and some mouse caspases are active in apoptosis and cell death and even in necrosis and inflammation. CASP Gene and orthologous enzymes have been identifies successfully in the signal transduction cascade and pathways.For cells, cell lines and tissues in culture till half confluency.Tissue, pathway, proteinase, peptidase, protease ,acrosin, lipoprotein, activator, caspase, trypsin, papain, esterase inhibitors are proteins or receptor ligands or receptor antagonists that bind to an enzyme receptor and decreases its activity. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. Not all receptor antagonist that bind to enzymes are inhibitors; enzyme activator ligands or agonists bind to enzymes and increase their enzymatic activity, while enzyme substrates bind and are converted to products in the normal catalytic cycle of the enzyme.