CTSB Mouse, Active
Description
What Is CTSB Mouse, Active?
CTSB Mouse, Active refers to the enzymatically active recombinant form of mouse cathepsin B (CTSB), a lysosomal cysteine protease. It is produced in Sf9 Baculovirus cells as a glycosylated polypeptide chain of 330 amino acids (18–339a.a.) with a molecular mass of 36.4 kDa . The protein includes an 8-amino-acid His tag at the C-terminus for purification . Its enzymatic activity (>2,000 pmol/min/μg) makes it critical for in vitro studies on proteolysis, extracellular matrix (ECM) degradation, and disease mechanisms.
Formulation
Neurologic Disease Models
CTSB elevation correlates with pathology in traumatic brain injury (TBI), ischemia, and neuroinflammatory disorders :
CTSB knockout (KO) mice show improved neurobehavioral outcomes and reduced inflammation .
Cancer and ECM Degradation
Apoptosis Regulation
| Study Model | Key Finding | Source |
|---|---|---|
| Mouse Granulosa Cells (GCs) | CTSB knockdown ↓ apoptosis by 50% (vs. controls) |
Applications in Biomedical Research
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Neurodegenerative Disease: CTSB contributes to β-amyloid peptide production in Alzheimer’s models; inhibition reduces Aβ plaques .
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Cancer Research: Role in ECM remodeling and pro-uPA activation for plasminogen-driven metastasis .
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Immunology: Modulates T/B cell apoptosis and Th1/Th2 polarization .
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Cardiovascular/Arthritis Studies: Linked to plaque rupture and joint inflammation .
Activity Measurement (Fluorometric)
| Step | Conditions | Source |
|---|---|---|
| Activation | 10 μg/mL in 25 mM MES, 1–5 mM DTT, pH 5.0 (3–15 min) | |
| Substrate | 20–40 μM Z-Leu-Arg-AMC/Z-Arg-Arg-AMC | |
| Detection | Ex/Em: 380/460 nm (kinetic, 5 min) |
Example Calculation:
Product Specs
To ensure stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advisable.
Repeated freezing and thawing of the product should be avoided.
Product Science Overview
Cathepsin B is synthesized as an inactive proenzyme and undergoes proteolytic processing to become an active enzyme. The active form of cathepsin B is a single, glycosylated polypeptide chain containing 330 amino acids, with a molecular mass of approximately 36.4 kDa . The enzyme is characterized by its ability to cleave peptide bonds, particularly at acidic pH levels found within lysosomes .
Cathepsin B is involved in various physiological processes, including protein degradation, antigen processing, and tissue remodeling. It is also implicated in pathological conditions such as cancer, inflammation, and neurodegenerative diseases. The enzyme’s activity is regulated by its localization within lysosomes and its interaction with specific substrates .
Recombinant cathepsin B (mouse) is produced using baculovirus expression systems in Sf9 insect cells. This method allows for the production of large quantities of the enzyme with high purity and activity. The recombinant enzyme retains the biochemical properties of the native enzyme, making it suitable for research and therapeutic applications .
Recombinant cathepsin B is widely used in biochemical and biomedical research. It serves as a valuable tool for studying the enzyme’s structure, function, and role in disease. Additionally, it is used in drug discovery and development, particularly in the design of inhibitors that target cathepsin B activity in pathological conditions .
