SCP0069
Caspase 1 Substrate
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About This Item
Productos recomendados
assay
≥95% (HPLC)
form
lyophilized
composition
Peptide Content, ≥87%
storage condition
protect from light
storage temp.
−20°C
Amino Acid Sequence
Ac-Trp-Val-Ala-Asp-AMC
Application
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 VAD (val-ala-asp) or WEAD (trp-glu-ala-asp) sequences. These substrates include: Ac-VAD-pNa (acetyl-Val-Ala-Asp-p-nitroanalide), chromogenic; Ac-VAD-AFC (acetyl-Val-Ala-Asp-AFC), fluorogenic; Ac-VAD-4-methoxy-2-naphtylamide (acetyl-Val-Ala-Asp-4-methoxy-2-naphtylamide); Ac-WVAD-pNa (acetyl-Trp-Val-Ala-Asp-p-nitroanalide), chromogenic; Ac-WVAD-AMC (acetyl-Trp-Val-Ala-Asp-7-amino-4-methylcoumarin), fluorogenic; Ac-WEAD-pNA (acetyl-Trp-Glu-Ala-Asp-p-nitroanalide), chromogenic; Ac-WEAD-AMC (acetyl-Trp-Glu-Ala-Asp-7-amino-4-methylcoumarin), fluorogenic; and MCA-YVADAP-DNP-K (MCA-Tyr-Val-Ala-Asp-Ala-Pro-DNP-Lys).
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
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
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
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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