Technical Data

C2087-27S
Clone Type
Polyclonal
Host
Rabbit
Source
Human
Isotype
IgG
Grade
Affinity Purified
Applications
E WB
Crossreactivity
Hu
Shipping Temp
Blue Ice
Storage Temp
-20°C
Rabbit Anti-Caspase 6 (Mch 2)

Apoptosis or programmed cell death is essential for normal tissue development and abnormal growth such as cancer, neurodegeneration, autoimmune diseases, and angiogenesis, etc. Apoptosis is driven by caspases (cysteine proteases that cleave after an aspartic acid residue). After the initial discovery of the first mammalian caspase 1 or ICE (interleukin 1 beta converting enzyme), a growing family of caspases 1-14 have been cloned and characterized. Caspases are synthesized as inactive zymogen or proenzyme forms (30-55kD), which upon apoptotic stimulation are proteolytically processed (self or by other proteins) in a sequential manner into their active heterotetrameric forms. The processed form consists of large subunit (17-20kD) and a small (10-12kD) subunits, which may associate to form an active enzyme. Functionally active caspases initiate a proteolytic cascade, capable of cleaving and activating numerous cellular targets including PARP, G4-GDI, DFF, MEKK, etc. On a functional basis, two categories of caspases have been defined: the initiator caspases (caspases-8, -9, and –10) are activated in the earlier phases of apoptosis, whereas the executioner caspases (caspases-3, -6, and –7) are activated by initiator caspases and are responsible for dismantling cellular components.

Caspase-6, (also known as ICE-6, MCH-2, CASP-6) (Zymogen 35-40kD) is mapped at human chromosome 4q25q25 and executes the final apoptotic phase. The processed form of human is a heterotetramer consisting of two large ~18kD and two small ~11kD subunits. Alternative splicing of human CASP-6 results in two isoforms: alpha (293aa) and beta (204aa) but beta isoform does not have protease activity. Mouse (276aa) and rat (277aa) and human CASP-6 proenzymes are activated by CASP-3, -8 or –10. Unlike CASP-3 and MCH-3, Hs CASP-6 (MCH-3) can cleave lamin-A and –C in their signature apoptotic fragments. CASP-6 mediates the shrinkage and fragmentation of nuclei. It is highly expressed in lung, liver, kidney, testis and heart; lower levels in spleen, skeletal muscle and brain.
Applications
Suitable for use in Western Blot and ELISA. Other applications not tested.
Recommended Dilution
Western Blotting (1-10ug/ml for affinity pure antibody using ECL technique). Will recognize 34kD Procaspase-6 and alternatively spliced 22kD isoform-beta. ELISA: Control peptide can be used to coat ELISA plates at 1ug/ml and detected with antibodies ( 0.5-1ug/ml for affinity pure). Optimal dilution determined by the researcher.
Storage and Stability
Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile ddH2O or PBS. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Immunogen
15aa peptide (250-264aa of alpha)/(161-175aa of beta) of Human Caspase-6 Interna lHuman Caspase-6 (Mol wt, ~34kD) was expressed in E.coli
Form
Supplied as a lyophilized powder from PBS, 0.05% sodium azide.
Purity
Purified by immunoaffinity chromatography.
Specificity
Human control peptide is 100% conserved in Human, mouse and rat caspase-6. Recognizes Caspase-6 in mouse, rat human, monkey, bovine, sheep, rabbit, dog, pig and hamster cells.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
(1) Nasir, J et al (1997) Mamm. Genome 8, 611; Munday,NA et al (1995) JBC 270, 15870; Faucheu, C. et al (1995) Eur J. Biochem. 236, 207; Fernandes-Alnemri T. et al (1994) JBC 269, 30761; LeBlanc, A. et al (1999) JBC 274, 23426; Stennicke, HR & Salvessen, GS (1997) 272, 25719.
USBio References
No references available
United States Biological | 4 Technology Way | Salem, MA 01970
Phone 800-520-3011 | Fax 978-594-8052 | Website www.usbio.net