Caspase 6

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Product Preparation
A synthetic peptide derived from C-terminus of human Caspase 6 protein. This sequence is identical to human rat and mouse species.
Caspases belong to the cysteine-aspartic acid protease (Caspase) family which plays a major role in the transduction of the apoptotic signal and execution of apoptosis in mammalian cells. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This protein could be processed by caspases 7, 8 and 10, and is thought to function as a downstream. Caspase 3 (CPP32) and Caspase 6 (Mch2) are the major active caspases in apoptotic cells, and are activated in response to distinct apoptosis-inducing stimuli and in all cell lines analyzed. Both CPP32 and Mch2 are present in apoptotic cells as multiple active species. Caspase-6 cleaves nuclear mitotic apparatus protein (NuMA) and mediates the shrinkage and fragmentation of nuclei.
The Rabbit IgG is purified by Epitope Affinity Purification
This antibody recognizes ~33 kDa of human Caspase 6 protein. It is cross react to human and mouse. The other species are not tested.
This affinity purified antibody is supplied in sterile Phosphate buffered saline (pH7.2) containing antibody stabilizer.
The antibodies are stable for 12 months from date of receipt when stored at –20oC. The antibodies can be stored at 2oC-8oC for one month without detectable loss of activity. Avoid repeated freezing-thawing cycles.
Gene ID
Applications/Suggested Working Dilutions
Western Blot
0.1-1 µg/ml
0.01-0.1 µg/ml
2-5 µg/ml
2-10 µg/ml
Flow cytometry
5-10 µg/ml
Order Info
Catalog #: 500-7194
Lot #: See the label
Size: 100 ug
Host: Rabbit
Isotyping: Rabbit IgG
Applications: WB
Reactivity: Hu, Rt, Ms
Price: $ 379.00
Van de Craen,M., Vandenabeele,P., Declercq,W., Van den Brande,I., Van Loo,G., Molemans,F., Schotte,P., Van Criekinge,W., Beyaert,R. and Fiers,W. Characterization of seven murine caspase family members. FEBS Lett. 403 (1), 61-69 (1997).
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