Mouse Cathepsin B Biotinylated Antibody Summary
His18-Phe339
Accession # P10605
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
Cathepsin B in Mouse Liver. Cathepsin B was detected in perfusion fixed frozen sections of mouse liver using Goat Anti-Mouse Cathepsin B Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF965) 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 staining was localized to cytoplasm in hepatocytes. View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
- 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.
- Berquin, I.M. and B.F. Sloane (1996) Adv. Exp. Med. Biol. 389:281.
Product Datasheets
Citations for Mouse Cathepsin B Biotinylated Antibody
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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Cathepsin D deficiency in mammary epithelium transiently stalls breast cancer by interference with mTORC1 signaling
Authors: S Ketterer, J Mitschke, A Ketscher, M Schlimpert, W Reichardt, N Baeuerle, ME Hess, P Metzger, M Boerries, C Peters, B Kammerer, T Brummer, F Steinberg, T Reinheckel
Nat Commun, 2020-10-12;11(1):5133.
Species: Mouse
Sample Types: Cell Lysates
Applications: Western Blot -
Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation.
Authors: Duncan EM, Muratore-Schroeder TL, Cook RG, Garcia BA, Shabanowitz J, Hunt DF, Allis CD
Cell, 2008-10-17;135(2):284-94.
Species: Human
Sample Types: Cell Lysates
Applications: Bioassay -
The secreted inhibitor of invasive cell growth CREG1 is negatively regulated by cathepsin proteases
Authors: Alejandro Gomez-Auli, Larissa Elisabeth Hillebrand, Daniel Christen, Sira Carolin Günther, Martin Lothar Biniossek, Christoph Peters et al.
Cellular and Molecular Life Sciences
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