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  • 產(chǎn)品名稱：Caspase-2,3Substrate-pNA

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  • 產(chǎn)品廠商：KamiyaBiomedical
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Caspase-2,3Substrate-pNA
詳情介紹：
Purpose Soluble in DMSO and aqueous buffers. We recommend preparing a stock solution in DMSO, and diluting into aqueous buffer shortly prior to use.
1. Lyse cells in 50 mM Tris-HCl, pH 7.5, 0.3% NP-40, 1.0 mM DTT, at a density of 2 X 10^6 /mL.
2. Assay 0.01 mL cell lysate in a final volume of 0.1 mL. Assay buffer is cell lysis buffer containing 0.2 mM substrate.
3. Incubate at 37°C for 0-3 hr. Take periodic readings of absorbance at 405 nm.
Sequence Acetyl-Val-Asp-Val-Ala-Asp-pNA, Ac-VDVAD-pNA
Specificity Substrate for caspase-2, 3.
Purity > 97 % by HPLC
Background Chromogenic paranitroanilide-peptide substrate for caspase-2 (ICH-1). Release of free pNA is monitored by absorbance at 405 nm (epsilon=9,160 M^-1 cm^-1 ). Caspase-2 (also known as ICH-1) is a member of the caspase family of cysteine proteases involved in apoptosis. It is a member of the Group II caspases, along with caspases-3 and - 7. Group II caspases prefer peptides of the DEXD-type as substrates. However, unlike caspases-3 and -7, Caspase-2 requires a P5 amino acid in the peptide for efficient cleavage. The similar substrate specificities of the Group II caspases suggests that their roles in cells are at least overlapping, if not completely redundant. The requirement for a fifth amino acid in substrates for Caspase-2 means that the DEVD-type, while serving as substrates for caspases-3 and -7, do not work with Caspase-2. For this reason, the Ac-VDVAD-pNA substrate is excellent for studying Caspase-2.
Molecular Weight 679 Da
Application Notes Assay of caspase activity in cell extracts.
Restrictions For Research Use only
Format Lyophilized
Storage RT
Background publications Talanian, Quinlan, Trautz, Hackett, Mankovich, Banach, Ghayur, Brady, Wong: "Substrate specificities of caspase family proteases." in: The Journal of biological chemistry, Vol. 272, Issue 15, pp. 9677-82, 1997 (PubMed).

Thornberry, Rano, Peterson, Rasper, Timkey, Garcia-Calvo, Houtzager, Nordstrom, Roy, Vaillancourt, Chapman, Nicholson: "A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis." in: The Journal of biological chemistry, Vol. 272, Issue 29, pp. 17907-11, 1997 (PubMed).

Duan, Orth, Chinnaiyan, Poirier, Froelich, He, Dixit: "ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B." in: The Journal of biological chemistry, Vol. 271, Issue 28, pp. 16720-4, 1996 (PubMed).

Srinivasula, Fernandes-Alnemri, Zangrilli, Robertson, Armstrong, Wang, Trapani, Tomaselli, Litwack, Alnemri: "The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32." in: The Journal of biological chemistry, Vol. 271, Issue 43, pp. 27099-106, 1996 (PubMed).

Faucheu, Diu, Chan, Blanchet, Miossec, Hervé, Collard-Dutilleul, Gu, Aldape, Lippke: "A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells." in: The EMBO journal, Vol. 14, Issue 9, pp. 1914-22, 1995 (PubMed).

Kamens, Paskind, Hugunin, Talanian, Allen, Banach, Bump, Hackett, Johnston, Li: "Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases." in: The Journal of biological chemistry, Vol. 270, Issue 25, pp. 15250-6, 1995 (PubMed).

Munday, Vaillancourt, Ali, Casano, Miller, Molineaux, Yamin, Yu, Nicholson: "Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases." in: The Journal of biological chemistry, Vol. 270, Issue 26, pp. 15870-6, 1995 (PubMed).