|Detection of Human Kallikrein 3/PSA by Western Blot. Western blot shows lysates of human prostate tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Kallikrein 3/PSA Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1344) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Kallikrein 3/PSA at approximately 31 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Kallikrein 3/PSA in Human Kidney Cancer Tissue. Kallikrein 3/PSA was detected in immersion fixed paraffin-embedded sections of human kidney cancer tissue using Goat Anti-Human Kallikrein 3/PSA Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1344) at 15 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 labeling was localized to the cytoplasm of cells in convoluted tubules. View our protocol for Chromogenic IHC Staining of immersion fixed paraffin-embedded Tissue Sections.|
Kallikrein 3, commonly known as prostate specific antigen (PSA), is a serine protease of the human tissue Kallikrein gene family (1). PSA is synthesized in the ductal and acinar epithelium of the prostate gland and secreted into the seminal plasma in high concentrations (0.5 - 2 g/L) (2). A small portion of PSA “leaks” into the systemic circulation, the levels of which increase significantly (30-fold) from prostate cancer tissue than normal prostate tissue (3). PSA has become a well established tumor marker that aids the diagnosis, staging, and follow up of prostate cancer.
The deduced amino acid sequence of human PSA consists of a signal peptide, a short pro region and a mature/active enzyme. The pro-enzyme is activated, possibly by active Kallikreins 2, 4 or 15 in vivo (4). rhPSA is activated by thermolysin, a zinc protease. The active PSA cleaves several tyrosyl peptide bonds in semenogelins I and II, which are the major gel-forming proteins produced by the seminal vesicles (5). Several inhibitors including serpin A3/ alpha 1-antichymotrypsin (ACT) and alpha 2-macroglobulin are known to form complexes with PSA.
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