Polyclonal antibody to Caspase-14

Apoptosis, or programmed cell death, is a common property of all multicellular organisms. The current dogma of apoptosis suggests that the components of the core celldeath machinery are integral to cells and widely conserved across species. Caspases are typically divided into 3 major groups, depending on the structure of their prodomain and their function. Group 1: inflammatory caspases (caspases 1, 4, 5, 11, 12, 14). Group II: initiator of apoptosis caspases (2, 8, 9). Group III: effector caspases (3, 6, 7). Caspases are constitutively expressed in almost all cell types as inactive proenzymes (zymogens: enzyme precursors which require a biochemical change to become active enzymes) that are processed and activated in response to a variety of pro-apoptotic or inflammatory stimuli. The procaspases (32-56 kDa) contain four domains: an N-terminal prodomain (2-25 kDa), a large subunit (p20: 17-21 kDa), a small subunit (p10: 10-13 kDa) and a short linker region between the large and small subunits. Caspase activation involves proteolytic processing of the proenzyme at specific aspartate residues between the domains. This results in removal of the prodomain as well as the linker region and formation of a heterodimer containing one large and one small subunit (p20-p10). Active caspases mediate cell death and inflammation through cleavage of particular cellular substrates that are involved in these processes. Caspase-14 activation has been implicated in keratinocyte senescence which leads to the cornified cell layer, suggesting a role for caspase-14 in epithelial cell differentiation. Tumor-specific alterations in caspase-14 expression have been found in epithelial malignancies, suggesting that caspase-14 plays a role in epithelial cell transformation. This antibody recognizes the proform of caspase-14 (~28-32 kDa), and the large (~14-21 kDa) and small (~10-11 kDa) of active/cleaved caspase-14.