218833
Caspase-6 Inhibitor XII, pep419
The Caspase-6 Inhibitor XII, pep419 controls the biological activity of Caspase-6. This small molecule/inhibitor is primarily used for Cancer applications.
Synonym(s):
Caspase-6 Inhibitor XII, pep419, Caspase inhibitor, pep419
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About This Item
Empirical Formula (Hill Notation):
C99H162N30O29S
Molecular Weight:
2268.59
UNSPSC Code:
12352200
Quality Level
assay
≥95% (HPLC)
form
powder
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
protect from light
color
white
solubility
water: 100 mg/mL
shipped in
ambient
storage temp.
−20°C
General description
An 18-mer synthetic peptide that acts as a selective, non-competitive inhibitor of caspase-6 (IC50 = 8.6 µM). Blocks the activity of processed caspase-6 as evidenced by its reduced ability to process VEID-AMC substrate. Exhibits only a trivial effect on caspase-9 and 7 and does not affect the activities of caspases 1, 2, 3, 4, 5, 8, and 10. Acts as an allosteric peptide ligand that binds outside the active site of the enzyme and impairs its activity. Pep419 is shown to bind as a dimer to an allosteric site of caspase-6 zymogen resulting in its tetramerizaton and stabilization. Its binding site is shown to be distinct from the substrate binding site of the enzyme. Electroporation has been shown to enable the entry of 5-carboxyfluorescein-labeled peptide into SKNAS bone marrow neuroblastoma cells.
Packaging
Packaged under inert gas
Warning
Toxicity: Standard Handling (A)
Sequence
Ac-TEKEKGRLHCVEWTILER-NH2
Other Notes
Stanger, K., et al. 2012. Nat. Chem. Bio.8, 655.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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Karen Stanger et al.
Nature chemical biology, 8(7), 655-660 (2012-06-12)
The caspases are a family of cytosolic proteases with essential roles in inflammation and apoptosis. Drug discovery efforts have focused on developing molecules directed against the active sites of caspases, but this approach has proved challenging and has not yielded
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