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Key Documents

400011

Sigma-Aldrich

Caspase-1 Inhibitor I, Cell-Permeable

The Caspase-1 Inhibitor I, Cell-Permeable controls the biological activity of Caspase-1. This small molecule/inhibitor is primarily used for Cancer applications.

Sinónimos:

Caspase-1 Inhibitor I, Cell-Permeable, ICE Inhibitor I, Cell-permeable, YVAD-CHO, Cell-permeable, Ac-AAVALLPAVLLALLAPYVAD-CHO

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About This Item

Fórmula empírica (notación de Hill):
C97H160N20O24
Peso molecular:
1990.43
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

assay

≥97% (HPLC)

form

solid

potency

1 nM Ki

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

color

white

solubility

DMSO: 5 mg/mL

shipped in

ambient

storage temp.

−20°C

General description

A cell-permeable inhibitor of caspase-1 (ICE; Interleukin-1β Converting Enzyme), caspase-4, and caspase-5. The C-terminal YVAD-CHO sequence of this peptide is a highly specific, potent, and reversible inhibitor of caspase-1 (Ki = 1 nM). The N-terminal sequence (amino acid residues 1-16) corresponds to the hydrophobic region (h-region) of the signal peptide of the Kaposi fibroblast growth factor (K-FGF) and confers cell-permeability to the peptide.
A cell-permeable inhibitor of caspase-1 (ICE; interleukin-1β converting enzyme). The C-terminal YVAD-CHO sequence of this peptide is a highly specific, potent, and reversible inhibitor of caspase-1 (Ki = 1 nM). The N-terminal sequence (residues 1-16) corresponds to the hydrophobic region (h-region) of the signal peptide of Kaposi fibroblast growth factor (K-FGF) and confers cell-permeability to the peptide.

Biochem/physiol Actions

Cell permeable: yes
Primary Target
Caspase-1
Product does not compete with ATP.
Reversible: yes

Warning

Toxicity: Standard Handling (A)

Sequence

Ac-Ala-Ala-Val-Ala-Leu-Leu-Pro-Ala-Val-Leu-Leu-Ala-Leu-Leu-Ala-Pro-Tyr-Val-Ala-Asp-CHO

Reconstitution

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 1 month at -20°C.

Other Notes

Garcia-Calvo, M., et al. 1998. J. Biol. Chem. 273, 32608.
Hilbi, H., et al. 1998. J. Biol. Chem. 273, 32895.
Thornberry, N.A., and Lazebnik, Y. 1998. Science 281, 1312.
Lin, Y.-Z., et al. 1996. J. Biol. Chem.271, 5305.
Lin, Y.-Z., et al. 1995. J. Biol. Chem.270, 14255.
Reiter, L.A. 1994. Int. J. Pept. Protein Res.43, 87.
Thornberry, N.A., et al. 1994. Biochemistry33, 3934.
Thornberry, N.A., et al. 1994. MethodsEnzymol. 244, 615.
Thornberry, N.A., et al. 1992. Nature 356, 768.

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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C C Teixeira et al.
American journal of physiology. Cell physiology, 281(3), C833-C839 (2001-08-15)
An elevation in inorganic phosphate (P(i)) concentration activates epiphyseal chondrocyte apoptosis. To determine the mechanism of apoptosis, tibial chondrocytes were treated with P(i), and nitrate/nitrite (NO/NO) levels were determined. P(i) induced a threefold increase in the NO/NO concentration; inhibitors of

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