SCP0068
Caspase 1 Substrate
≥92% (HPLC), lyophilized
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About This Item
Produits recommandés
product name
Caspase 1 Substrate, ≥92% (HPLC)
Pureté
≥92% (HPLC)
Forme
lyophilized
Composition
Peptide Content, ≥80%
Conditions de stockage
protect from light
Température de stockage
−20°C
Amino Acid Sequence
Ac-Trp-Glu-Ala-Asp-pNA
Application
Caspase 1 is a cysteine protease activator of inflammatory processes which may be detected using a variety of chromogenic and fluorogenic peptide substrates built 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).
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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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