Western Blot: Caspase-14 Antibody [NB100-56126] - Analysis of Caspase-14. Tissue lysates (50 ug/lane) and recombinant human Caspase-14 were (Hu C14, 15 ng) were western blotted with Caspase-14 antibody at 1:2000. The ...read more
Immunohistochemistry: Caspase-14 Antibody [NB100-56126] - Immunohistochemistry-Paraffin: Caspase-14 Antibody [NB100-56126] - Tissue sections of mouse skin at E17 stained using this antibody at 1:500.
Immunohistochemistry-Paraffin: Caspase-14 Antibody [NB100-56126] - Formalin-fixed paraffin-embedded sections from a human ovarian cancer tissue microarray stained for Caspase-14 expression using this antibody at ...read more
Immunohistochemistry-Paraffin: Caspase-14 Antibody [NB100-56126] - Tissue sections of human cervix stained using this antibody at 1:2000. A. Normal cervix (squamous epithelium). B. CIN1 (low-grade squamous ...read more
Cross reacts with Dog, Gerbil, Human, Mouse and Rat.
Packaging, Storage & Formulations
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Neat whole antisera
0.02% Sodium Azide
Alternate Names for Caspase-14 Antibody
apoptosis-related cysteine protease
caspase 14, apoptosis-related cysteine peptidase
caspase 14, apoptosis-related cysteine protease
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 cell-death machinery are integral to cells and widely conserved across species. Caspases, a family of cysteinyl aspartate-specific proteases, are integral components of the cell death machinery (reviewed in Siegal, 2006; and Lavrik et al, 2005). They play a central role in the initiation and execution of apoptotic cell death and in inflammation. 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 (caspases 2, 8, 9). Group II: effector caspases (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). The active caspase is a tetramer composed of two heterodimers (p202-p102). 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 (Pistritto et al. 2002). Terminal differentiation of keratinocytes has some features of classical apoptosis including DNA fragmentation, nuclear condensation, and induction of cross-linking transglutaminases. Tumor-specific alterations in caspase-14 expression have been found in epithelial malignancies, suggesting that caspase-14 plays a role in epithelial cell transformation. The caspase-14 NB100-56126 antibody recognizes the proform of caspase-14 (approx. 28-32 kDa), and the large (approx. 14-21 kDa) and small (approx. 10-11 kDa) of active/cleaved caspase-14.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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