- CITATIONS: 5
|Application ||IHC-P, DB, E|
|Other Accession||P55213, Q95ND5, P70677, Q08DY9|
|Predicted||Bovine, Mouse, Pig, Rat|
|Calculated MW||31608 Da|
|Antigen Region||149-175 aa|
|Other Names||Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1, Caspase-3 subunit p17, Caspase-3 subunit p12, CASP3, CPP32|
|Target/Specificity||This Cleaved antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 149-175 amino acids from human Cleaved.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Cleaved-CASP3 (Asp175) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.|
|Tissue Location||Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system|
Provided below are standard protocols that you may find useful for product applications.
CASP3 encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease.
Mei, Y., et al. Mol. Cell 37(5):668-678(2010) Sohn, E.J., et al. Cancer Res. 70(3):1154-1163(2010) Karamitopoulou, E., et al. Pathology 42(1):37-42(2010)
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