Caspase 3 Vsl Cd107 Ctl

Description: Minimum order quantity: 1 unit of 1KIT

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: This recombinant Caspase-3 antibody reacts to human full length caspase-3 (35 kDa) and the large fragment of caspase-3 resulting from cleavage (17 kDa).

Description: Caspase-3, also known as YAMA, CPP32 or APOPAIN, is a member of the cysteine-aspartic acid protease family known to interact with family members -8 and -9. It is encoded by the CASP3 gene. Tiso et al.(1996) used radiation hybrid mapping to localize the gene to human chromosome 4q33-q35.1. Fernandes-Alnemri et al.(1994) found that overexpression of CASP3 in insect cells induced apoptosis. Coexpression of the two CASP3 subunits in insect cells also resulted in apoptosis. Tewari et al.(1995) showed that purified human CASP1 cleaved the CASP3 proenzyme into a proteolytically active form and that activated Caspase-3 cleaved PARP into the 85-kD apoptotic form.

Description: Cysteine-aspartic acid protease 3, also known as Apopain, CPP32, CPP32B, and YAMA, is a member of the cysteine-aspartic acid protease family. Western blot analysis of three cell lines revealed the prominent CASP3 band at 32 kD and 20 kD. Several human cancer cell lines showed coexpression of both variants at the mRNA and protein levels. Overexpression of the catalytically inactive Caspase-3 by human kidney cells offered some resistance to inducers of apoptosis, and CASP3 accumulation could be enhanced with addition of proteasome inhibitors. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Alternative splicing of this gene results in two transcript variants that encode the same protein. Orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts. Nicholson et al. developed a potent peptide aldehyde inhibitor and showed that it prevented apoptotic events in vitro, suggesting that the protein is important for the initiation of apoptotic cell death.

Description: Caspase-3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located at 4q35 encodes a protein that 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 that 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 Alzheimers disease. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.

Description: Caspase-3 is an enzyme which interacts with Survivin, XIAP, CFLAR, CASP8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that is a member of the cysteine-aspartic acid protease family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. They exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. CASP3 is the predominant cysteine-aspartic acid protease involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimers disease. And protein activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the proteins influence on bone mineral density should be considered in any in vivo application of Caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.

Description: Caspase 3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that 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 that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. 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. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.

Description: Caspase 3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that 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 that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. 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. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.

Description: Purified recombinant Human Caspase 3 protein

Description: Purified recombinant Human Caspase 3 protein

Description: Purified recombinant Human Caspase 3 protein

Description: Purified recombinant Human Caspase 3 protein

Description: Recombinant Human Caspase-3(CASP3),partial expressed in E.coli

Description: Rabbit polyclonal Caspase 3 antibody

Description: Rabbit polyclonal Caspase 3 antibody