Description: Protein

Description: Mouse

Description: Caspase-12 Antibody: (Small)Three distinct signaling pathways lead to programmed cell death (apoptosis). The death receptor and mitochondrion pathways are the main, in which the key apoptotic proteases capase-8 and caspase-9, respectively, are involved. The endoplasmic reticulum (ER) stress is the third apoptotic pathway and caspase-12 is involved. Caspase-12 is localized to the ER but not to cytoplasm or mitochondrion. Caspase-12 is activated by ER stress, including disruption of ER calcium homeostasis, and mediates ER stress-induced apoptosis. Caspase-12 is co-localized to the ER with several proteins that are involved in Alzheimer's disease including gamma-secretase presenilin and beta-amyloid precursor protein (APP). Caspase-12 mediates cytotoxicity induced by amyloid-beta. Caspase-12 is ubiquitously expressed in mouse tissues.

Description: Caspase-12 Antibody: (Small)Three distinct signaling pathways lead to programmed cell death (apoptosis). The death receptor and mitochondrion pathways are the main, in which the key apoptotic proteases capase-8 and caspase-9, respectively, are involved. The endoplasmic reticulum (ER) stress is the third apoptotic pathway and caspase-12 is involved. Caspase-12 is localized to the ER but not to cytoplasm or mitochondrion. Caspase-12 is activated by ER stress, including disruption of ER calcium homeostasis, and mediates ER stress-induced apoptosis. Caspase-12 is co-localized to the ER with several proteins that are involved in Alzheimer's disease including gamma-secretase presenilin and beta-amyloid precursor protein (APP). Caspase-12 mediates cytotoxicity induced by amyloid-beta. Caspase-12 is ubiquitously expressed in mouse tissues.

Description: Available in various conjugation types.

Description: CASP8 is also known as CAP4, MACH or MCH5. This gene encodes 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 composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. In addtion, this protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.

Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human Caspase-12 (Small). This antibody is tested and proven to work in the following applications: