Spinesin in Mouse Brain. Spinesin was detected in perfusion fixed frozen sections of mouse brain (cerebellum) using Goat Anti-Mouse Spinesin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1928) 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 neurons in the granular cell layer. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
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.
Spinesin, encoded by the TMPRSS5 gene, is a new member of type II transmembrane serine proteases (TTSPs) (1). Mouse Spinesin contains the following structural domains: a short N-terminal cytoplasmic tail, a transmembrane domain, a stem region and a serine protease domain (2). The domain structure of Spinesin is common to other TTSPs, many of which have additional domains. The stem region of Spinesin contains a scavenger receptor-like domain. There could be 4 types of transcripts due to alternative splicing (3). Type 4 predicts 10 extra amino acids at the N-terminus as compared to type 3. The ectodomain corresponding to type 3 (residues 61‑445) or type 4 (residues 71‑455) was expressed and purified as a single chain pro-enzyme. By SDS-PAGE, the pro-enzyme migrates as multiple forms, possibly due to differential glycosylation. The pro-enzyme can be activated by trypsin treatment. The resulting enzyme is active and its activity is measured as described above. The activated enzyme is a disulfide bond-linked dimer.
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Yamaguchi, Y. et al. (2002) J. Biol. Chem. 277:6806.
Watanable, Y. et al. (2004) Biochem. Biophys. Res. Commun. 324:333.
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