Human Matriptase/ST14 Catalytic Domain Biotinylated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Intracellular Staining by Flow Cytometry View Larger

Detection of Matriptase/ST14 in PC‑3 Human Cell Line by Flow Cytometry. PC-3 human prostate cancer cell line was stained with Sheep Anti-Human Matriptase/ST14 Catalytic Domain Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF3946, filled histogram) or isotype control antibody (BAF020), followed by Streptavidin-Phycoerythrin (Catalog # F0040). To facilitate intracellular staining, cells were fixed with paraformaldehyde and permeabilized with saponin.

Preparation and Storage

Background: Matriptase/ST14

Human matriptase, encoded by the ST14 (suppression of tumorogenicity 14) gene, is also known as tumor associated differentially expressed gene 15 protein/TADG‑15), epithin, and membrane-type serine protease 1/MT-SP1 (1). Predicted to have a significant role in tumor biology, matriptase may be a novel target for anti-cancer therapy (2). However, expressed in most human epithelia, matriptase is also important in several physiological processes (1). For example, it activates prostasin to initiate a protease cascade that is essential for epidermal differentiation (3), and it converts a single-chain IGFBP-rp1 into the two-chain form (4).

Matriptase is a type II transmembrane serine protease with a complex modular structure (1). The 855 amino acid (aa) sequence of human matriptase consists of a cytoplasmic tail (aa 1-55), a transmembrane domain (aa 56-76), and an extracellular portion (aa 77-855). The latter contains the following domains: SEA (aa 86-201), two CUBs (aa 214-334 and 340-447), four LDLRAs (aa 452-486, 487-523, 524-560, and 566-603), and a serine protease (aa 615-855). The physiological activation of the single-chain zymogen requires the cleavage at the SEA domain within the ER or Golgi, association with HAI-1, which facilitates the transport of the protease to the cell surface, and auto-cleavage at QAR-V(615)VGG (1). The activated matriptase is inhibited by HAI-1, and the resulting HAI-1 complex can be shed from the cell surface (1). R&D Systems rhST14 corresponds to the catalytic domain, and is inhibited effectively by rhHAI-1 and rhHAI-2A (R&D Systems, Catalog # 1048-PI and 1106-PI).

Product Datasheets

Related Research Areas

• Cancer Biomarkers
• Search Bioprocessing Enzymes
• Serine Proteases and Regulators