SCP0073
Caspase 1 Substrate (ICE), fluorogenic
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About This Item
Fórmula empírica (Notação de Hill):
C35H41N5O12
Peso molecular:
723.73
Código UNSPSC:
12352202
NACRES:
NA.32
Produtos recomendados
Ensaio
≥95% (HPLC)
Formulário
lyophilized
composição
Peptide Content, ≥75%
condição de armazenamento
protect from light
temperatura de armazenamento
−20°C
Amino Acid Sequence
Ac-Tyr-Glu-Val-Asp-AMC
Aplicação
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.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
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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