Western blot analysis of CASP14. Tissue lysates (50 ug/lane) and recombinant human CASP14 were (Hu C14, 15 ng) were western blotted with CASP14 polyclonal antibody (Cat # PAB0250) at 1 : 2000. The antisera detected both the proform of CASP14, and the large and small subunits of active/cleaved CASP14.
Formalin-fixed paraffin-embedded sections from a human ovarian cancer tissue microarray stained for CASP14 expression. Using CASP14 polyclonal antibody (Cat # PAB0250) at 1 : 2000. Low (A) and high (B) stage ovarian tumor tissue cores. High magnification from areas of the tissue cores (A1 and B1) . Decreased CASP14 expression was seen in the high grade, compared to the low grade tumor. Hematoxylin-eosin counterstain.
Formalin-fixed paraffin-embedded tissue sections of human cervix stained for CASP14 expression. Using CASP14 polyclonal antibody (Cat # PAB0250) at 1 : 2000. A. Normal cervix (squamous epithelium) . B. CIN1 (low-grade squamous intraepithelial lesion, mild dysplasia) . C. CIN2 (high-grade squamous intraepithelial lesion, moderate dysplasia) . D. CIN3 (high-grade squamous intraepithelial lesion ; severe dysplasia-carcinoma in situ) . In normal cervi, CASP14 staining was found most in the midzone layer, but was absent from the basal/parabasal cell layer where mitotically active cells are known to reside. This suggests induction of CASP14 expression with differentiation. CASP14 expression declined progressively during malignant transformation as the histologic severity of the cervical atypia advanced from CIN1 to CIN3. Hematoxylin-eosin counterstain.
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 which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This caspase has been shown to be processed and activated by caspase 8 and caspase 10 in vitro, and by anti-Fas agonist antibody or TNF-related apoptosis inducing ligand in vivo. The expression and processing of this caspase may be involved in keratinocyte terminal differentiation, which is important for the formation of the skin barrier. [provided by RefSeq