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  • 產(chǎn)品名稱：Caspase-4,5,9Substrate-pNA

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  • 產(chǎn)品廠商：KamiyaBiomedical
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Caspase-4,5,9Substrate-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-Leu-Glu-His-Asp-pNA.TFA, Ac-LEHD-pNA
Specificity Serves equally well as a substrate for Caspases-4, -5, and -9. Can also serve as a weak substrate for Caspases-1, -2, -6, and -8 at an efficiency of 30-40% .
Purity > 97 % by HPLC
Background TFA salt of a paranitroanilide- peptide substrate for caspases-4, -5, and -9. Release of free pNA is monitored by absorbance at 405 nm (epsilon=9,160 M^-1 cm^-1 ). Caspase-4 (also known as ICErel-II, TX, or ICH- 2), Caspase-5 (also known as ICErel-III or TY), and Caspase-9 (also known as ICE-LAP6 or Mch6) are members of the caspase family of cysteine proteases involved in apoptosis. Caspases-4 and -5 belong to Group I (along with caspase-1), which prefer the tetrapeptide substrate sequence WEHD and are thought to be involved in inflammation through the maturation of pro-IL-1beta. Their role in apoptosis, however, is unclear. Caspase-9 is a member of Group III, which prefer the substrate sequence (L/V)jEXD. Since Caspase-9 has a strict requirement for His in the P4 position, it is not unexpected that the LEHD inhibitor sequence would work well on this caspase. The Group III caspases optimal recognition sequence resembles the activation sites within several effector caspase proenzymes, implicating the Group III enzymes as upstream components in the proteolytic cascade that amplifies the death signal.
Molecular Weight 788 Da (with TFA salt). 674 Da (without TFA salt).
Application Notes For in vitro assays of Caspases-4, -5, and -9 activity. Can be used with purified or partially purified enzymes, or possibly with crude cell lysates (if the Caspase-4,5,9 Inhibitor is included to determine background protease activity).
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).