產(chǎn)品詳情

  • 產(chǎn)品名稱：Caspase-6FluorogenicSubstrate

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  • 產(chǎn)品廠商：KamiyaBiomedical
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Caspase-6FluorogenicSubstrate
詳情介紹：
Purpose Fluorometer calibration: The fluorometer is calibrated using known concentrations of free AFC (Excitation = 400 nm, Emission = 505 nm) to generate a standard curve of fluorescence versus μ-moles AFC. Samples: Can be either purified or partially purified enzyme preparations. Application to crude cell lysates has not been confirmed. If crude cell lysates are to be assayed, the non- specific protease background must be determined using our Caspase-6 Inhibitor.
Sequence Ac-Val-Glu-Ile-Asp-AFC, Ac-VEID-AFC
Specificity Highly specific substrate for Caspase-6. May be weak substrate for Caspases-1 and -3.
Background Peptide substrate labeled at the carboxy end with AFC (7-amino-4-trifluoromethyl coumarin). Designed to measure Caspase-6 activity in vitro. Caspase-6 (also known as Mch2) is a member of the caspase family of cysteine proteases involved in apoptosis. It is a member of the Group III caspases (6, 8, and 9) which prefer the (L/V)EXD sequence as a substrate. Caspase-6 prefers a hydrophobic amino acid at P4, along with caspases-1 and -4, as opposed to the preference for Asp seen with caspases-2, -3, and -7. This is at odds with the gene sequence alignment that predicts Caspase-6 is more closely related to caspases-3 and -7 than to caspase-1. The preference by Caspase-6 for beta-branched amino acids in P4 fits well with the one known natural substrate, lamin A, and distinguishes it from caspases-1 and -4. Reconstitution experiments indicate that Caspase-6 activates caspases-3 and -7 and is therefore part of the proteolytic cascade that initiates apoptosis.
Molecular Weight 727.69 Da
Application Notes For in vitro assays of Caspase-6 activity. Can be used with purified or partially purified enzymes or possibly with crude cell lysates (if the Caspase-6 Inhibitor is included to determine background protease activity).
Restrictions For Research Use only
Storage -20 °C
Background publications Takahashi, Hirata, Yonehara, Imai, Lee, Moyer, Turner, Mesner, Okazaki, Sawai, Kishi, Yamamoto, Okuma, Sasada: "Affinity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and CrmA-sensitive caspase-8." in: Oncogene, Vol. 14, Issue 23, pp. 2741-52, 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).

Fernandes-Alnemri, Litwack, Alnemri: "Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family." in: Cancer research, Vol. 55, Issue 13, pp. 2737-42, 1995 (PubMed).