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product name
Caspase1 Substrate,
Assay
≥95% (HPLC)
form
lyophilized
composition
Peptide Content, ≥85%
storage condition
protect from light
storage temp.
−20°C
Amino Acid Sequence
MCA-Tyr-Val-Ala-Asp-Ala-Pro-DNP-Lys
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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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)
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
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
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