Mouse anti Human Caspase-6
| Code | Size | Price |
|---|
| EXA-X1173M | 100 ug | £316.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Mouse
Antibody Isotype: IgG
Antibody Clonality: Monoclonal
Antibody Clone: MCH2 14 1-190
Regulatory Status: RUO
Target Species: Human
Application: Western Blot (WB)
Shipping:
Ship at ambient temperature freeze upon arrival
Storage:
Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles
Further Information
Applications Description:
Detects proenzyme form of human Caspase-6 by Western blot. Optimal concentration should be evaluated by serial dilutions.
Background:
Caspase-6 (Cysteine-Requiring Aspartate Proteases) is part of a family of intracellular cysteine proteases that cleave their substrates after aspartic acid residues. These proteases play an integral role in inducing apoptosis in cells. Procaspase-6 (Mch2), a member of the ICE/ced-3 subfamily, is an inactive proenzyme that is activated to form caspase-6 by proteolytic cleavage at certain aspartic acid residues. During cleavage, the N-terminal is removed and the proenzyme is converted into a large (p18) and small (p11) subunits. Caspase-6 has two isoforms, and , produced by alternative splicing. Over-expression of the isoform of caspase-6 without its prodomain can induce apoptosis. The isoform does not seem to display proteolytic activity. Together with caspases-3 and -7, the isoform of caspase-6 is classified as an effector/execution caspase. Caspase-3, caspase-8 and caspase-10 can cleave procaspase-6. Active caspase-6 cleaves several other proteins such as lamins, NuMa and Keratin 18. A possible cleavage of caspases-8 and -10 in cytochrome-C dependent apoptosis was reported recently.
Caution:
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
Concentration:
See vial for concentration
Field of Interest:
Apoptosis
Formulation:
Provided as solution in phosphate buffered saline with 0.08% sodium azide
Functional Analysis:
Western Blotting
Immunogen:
Hybridoma produced by the fusion of splenocytes from mice immunized with recombinant human capase-6 protein and mouse myeloma cells.
Positive Control:
MCF-7 cell lysate
Product Form:
Unconjugated
Product Stability:
Products are stable for one year from purchase when stored properly
Purification Method:
Protein A/G Chromatography
Synonyms:
Cysteine-requiring Aspartate Protease-6; Apoptotic protease Mch-2
UniProt:
P55212
References
1. Kidd, V.J., Proteolytic activities that mediate apoptosis. Annu. Rev. Physiol. 1998, 60, 533-573
2. Fernandes ? Alnemri, T., et al., Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. Cancer Res. 1995, 55, 2737-2742
3. Orth, K., et al., The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 1996, 271, 16443
4. Hirata, H., et al., Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. J. Exp. Med. 1998, 187, 587-600
5. Slee, E. A., et al., Ordering the cytochrome c-initiated caspase cascade: hierarchial activation of caspases-2, -3, -6, -7, -8 and -10 in a caspase-9-dependent manner. J. Cell Biol., 144, 281 (1999)
6. Cohen, G.M., et al. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-16
2. Fernandes ? Alnemri, T., et al., Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. Cancer Res. 1995, 55, 2737-2742
3. Orth, K., et al., The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 1996, 271, 16443
4. Hirata, H., et al., Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis. J. Exp. Med. 1998, 187, 587-600
5. Slee, E. A., et al., Ordering the cytochrome c-initiated caspase cascade: hierarchial activation of caspases-2, -3, -6, -7, -8 and -10 in a caspase-9-dependent manner. J. Cell Biol., 144, 281 (1999)
6. Cohen, G.M., et al. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-16