Detection of Matriptase/ST14 in PC‑3 Human Cell Line by Flow Cytometry.
PC‑3 human prostate cancer cell line was stained with Mouse Anti-Human Matriptase/ST14 Catalytic Domain Monoclonal Antibody (Catalog # MAB3946, filled histogram) or isotype control antibody (Catalog # MAB002, open histogram), followed by Phycoerythrin-conjugated Anti-Mouse IgG F(ab')2 Secondary Antibody (Catalog # F0102B). To facilitate intracellular staining, cells were fixed with paraformaldehyde and permeabilized with saponin.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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).
List, K. et al. (2006) Mol. Med. 12:1.
Uhland, K. (2006) Cell. Mol. Life Sci. 63:2968.
Netzel-Arnett, S. et al. (2006) J. Biol. Chem. 281:32941.
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