Detection of Human, Mouse, and Rat Cathepsin X/Z/P by Western Blot. Western blot shows lysates of K562 human chronic myelogenous leukemia cell line, RAW 264.7 mouse monocyte/macrophage cell line, and NR8383 rat alveolar macrophage cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/|
Mouse/Rat Cathepsin X/Z/P Antigen Affinity-purified Polyclonal Antibody (Catalog # AF934) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Cathepsin X/Z/P at approximately 34 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
|Cathepsin X/Z/P in Human Breast and Breast Cancer Tissue. Cathepsin X/Z/P was detected in immersion fixed paraffin-embedded sections of normal human breast and breast cancer tissue using Goat Anti-Human/Mouse/Rat Cathepsin X/Z/P Antigen Affinity-purified Polyclonal Antibody (Catalog # AF934) at 3 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to stromal and endothelial cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
|Detection of Human Cathepsin X/Z/P by Simple WesternTM. Simple Western lane view shows lysates of HeLa human cervical epithelial carcinoma cell line, loaded at 0.2 mg/mL. A specific band was detected for Cathepsin X/Z/P at approximately 36 kDa (as indicated) using 5 µg/mL of Goat Anti-Human/Mouse/Rat Cathepsin X/Z/P Antigen Affinity-purified Polyclonal Antibody (Catalog # AF934) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.|
Cathepsin X (also known as Cathepsin Z and P) is a cysteine protease of the papain family (1‑5). Compared to other members of the papain family, Cathepsin X has a short proregion and unique insertions. The cysteine residue in the proregion forms a covalent and reversible bond with the active site cysteine residue (6). Acting as a carboxypeptidase, Cathepsin X displays a unique specificity (7‑10). It is ubiquitously expressed in human tissues and conserved in other species such as mouse, nematode and echiuran. The nematode enzyme is apparently involved in molting of third stage larvae (11).
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