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Merck

SCP0073

Sigma-Aldrich

カスパーゼ1基質(ICE)、蛍光発生基質

≥95% (HPLC), lyophilized

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About This Item

実験式(ヒル表記法):
C35H41N5O12
分子量:
723.73
UNSPSCコード:
12352202
NACRES:
NA.32

製品名

カスパーゼ1基質(ICE)、蛍光発生基質,

アッセイ

≥95% (HPLC)

フォーム

lyophilized

組成

Peptide Content, ≥75%

保管条件

protect from light

保管温度

−20°C

Amino Acid Sequence

Ac-Tyr-Glu-Val-Asp-AMC

アプリケーション

Caspase 1 is a cysteine protease activator of inflammatory processes which may be detected using a variety of chromogenic and fluorogenic peptide substrates build around the YEVD (Tyr-Glu-Val-Asp) sequence. These substrates include: Ac-YEVD-pNa (Ac-Tyr-Glu-Val-Asp-p-nitroanalide), chromogenic and Ac-YEVD-AMC (Ac-Tyr-Glu-Val-Asp-7-amino-4-methylcoumarin), fluorogenic.

保管分類コード

11 - Combustible Solids

WGK

WGK 3

引火点(°F)

Not applicable

引火点(℃)

Not applicable


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Eve-Lyne Marchand et al.
Circulation research, 92(7), 777-784 (2003-03-08)
Blockade of angiotensin type 1 (AT1) receptors induces smooth muscle cell (SMC) death and regression of aortic hypertrophy in spontaneously hypertensive rats (SHR). We postulated that SMC death and vascular remodeling in this model may be attenuated by z-Val-Ala-Asp(OMe)-CH2F (z-VAD-fmk)
F Martinon et al.
Cell death and differentiation, 14(1), 10-22 (2006-09-16)
Fifteen years have passed since the cloning and characterization of the interleukin-1beta-converting enzyme (ICE/caspase-1), the first identified member of a family of proteases currently known as caspases. Caspase-1 is the prototypical member of a subclass of caspases involved in cytokine
Annamaria Vezzani et al.
Current opinion in investigational drugs (London, England : 2000), 11(1), 43-50 (2010-01-05)
Epilepsy is a disabling neurological disorder that is characterized by recurring, unprovoked seizures. Drug-resistant epilepsy affects approximately 30% of individuals with epilepsy; thus, one of the main challenges for epilepsy therapy is the development of alternative anticonvulsant approaches. The discovery
Jerry Shen et al.
Atherosclerosis, 210(2), 422-429 (2010-01-12)
The preferred amino acids in the proteolytic sites have been considered to be similar between caspase-1 and caspase-9, which do not support their differential functions in inflammatory pyroptosis and apoptosis. We attempted to solve this problem. We analyzed the flanking

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