Detects mouse Cathepsin B in direct ELISAs and Western blots. In direct ELISAs, approximately 25% cross-reactivity with recombinant human Cathepsin B is observed and less than 5% cross-reactivity with recombinant mouse (rm) Cathepsin A, rmCathepsin C, and rmCathepsin D is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant mouse Cathepsin B His18-Phe339 Accession # P10605
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Measured by its ability to neutralize Recombinant Mouse Cathepsin B (0.1 µg/mL, Catalog # 965-CY) cleavage of the fluorogenic peptide substrate Z-LR-AMC (10 µM, Catalog # ES008). The Neutralization Dose (ND50) is typically 0.33 µg/mL.
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.
Cathepsin B in Mouse Thymus. Cathepsin B was detected in perfusion fixed frozen sections of mouse thymus using 5 µg/mL Goat Anti-Mouse Cathepsin B Antigen Affinity-purified Polyclonal Antibody (Catalog # AF965) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). 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.
Background: Cathepsin B
Cathepsin B is the first described member of the family of lysosomal cysteine proteases (1). Cathepsin B possesses both endopeptidase and exopeptidase activities, in the latter case acting as a peptidyl-dipeptidase. It is known to process a number of proteins, including pro and active caspases, prorenin and secretory leucoprotease inhibitor (SLPI) (2‑4). Therefore, Cathepsin B may play a role in activation and inactivation of caspases, activation of renin and inactivation of SLPI, the key steps in apoptosis, angiotensin production, and progression of emphysema, respectively. Because of its increased levels and redistribution in human and animal tumors, Cathepsin B may also have a role in invasion and metastasis (5). In addition to the lysosome, Cathepsin B can be secreted or associated with plasma membrane, cytoplasm, and nucleus. It is synthesized as a preproenzyme. Following removal of the signal peptide, the inactive proenzyme undergoes further modifications including removal of the pro region to result in the active enzyme (5).
Mort, J.S. (2004) in Handbook of Proteolytic Enzymes (Barrett, A.J. et al. eds.) p. 1079, Academic Press, San Diego.
Vancompernolle, K. et al. (1998) FEBS Lett. 438:150.
Jutras, I. and T.L. Reudelhuber (1998) FEBS Lett. 443:48.
Taggart, C.C. et al. (2001) J. Biol. Chem. 276:33345.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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