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Product List
CTSL Mouse
Cathepsin-L Mouse Recombinant
Recombinant CTSL from Mouse, produced in Sf9 insect cells using a Baculovirus expression system, is a single glycosylated polypeptide chain. It consists of 325 amino acids (18-334a.a.), resulting in a molecular weight of 36.8kDa. However, on SDS-PAGE, the apparent molecular size will be approximately 40-57kDa.
The CTSL protein is engineered with an 8 amino acid His tag at its C-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs 
Cat. No.
BT30670
Source
Sf9,
Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.
CTSD Human
Cathepsin-D Human Recombinant
Produced in HEK293 cells, CTSD is a single, glycosylated polypeptide chain. It comprises 398 amino acids (21-412 a.a.) and has a molecular weight of 43.4kDa. The protein is expressed with a 6 amino acid His tag at the C-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
CTSD Mouse
Cathepsin-D Mouse Recombinant
CTSD, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular mass of 44.0kDa. The protein consists of 398 amino acids (specifically, amino acids 21 to 410) and appears on SDS-PAGE at a size of approximately 40-57kDa. This CTSD variant includes an 8 amino acid His tag at its C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30483
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution that has been sterilized by filtration.
CTSE Human
Cathepsin-E Human Recombinant
Recombinant human CTSE, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 330 amino acids (residues 57-363). It has a molecular mass of 35.4 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
CTSF Human
Cathepsin-F Human Recombinant
CTSF Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (271-484) and having a molecular mass of 26kDa. CTSF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30577
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
CTSA Mouse
Cathepsin-A Mouse Recombinant
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Mouse CTSA, expressed in Sf9 Insect cells, is a single, glycosylated polypeptide chain containing 459 amino acids
(24-474 a.a.) with a predicted molecular mass of 52.4 kDa. The recombinant protein appears as a band of approximately 50-70 kDa on SDS-PAGE due to glycosylation. The CTSA protein is engineered with an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques. |
Shipped with Ice Packs
Cat. No.
BT30295
Source
Sf9 Insect cells.
Appearance
Sterile filtered colorless solution.
CTSB Mouse
Cathepsin-B Mouse Recombinant
Recombinant CTSB Mouse, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 330 amino acids (18-339a.a.) with a molecular weight of 36.4kDa. On SDS-PAGE, the apparent molecular size will be approximately 28-40kDa. The protein is expressed with an 8 amino acid His tag located at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30368
Source
Sf9,
Baculovirus cells.
Appearance
Clear, sterile solution after filtration.
CTSB Mouse, Active
Cathepsin-B Mouse Recombinant, Active
CTSB Mouse Recombinant, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 330 amino acids (18-339a.a.) and has a molecular mass of 36.4kDa. On SDS-PAGE, the apparent molecular size will be approximately 28-40kDa.
The CTSB protein is expressed with an 8 amino acid His tag at the C-Terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30406
Source
Sf9, Baculovirus cells.
Appearance
Sterile, clear solution that has undergone filtration.
Introduction
Definition and Classification
Cathepsins are a family of proteases (enzymes that degrade proteins) found in all animals and other organisms. The term “cathepsin” is derived from the Greek words “kata-” meaning “down” and “hepsein” meaning "boil" . These enzymes are primarily located in lysosomes, where they play a crucial role in protein degradation. Cathepsins are classified into three main types based on their catalytic mechanisms: cysteine proteases, aspartic proteases, and serine proteases .
Biological Properties
Biological Functions
Cathepsins are involved in several primary biological functions:
Modes of Action
Regulatory Mechanisms
The expression and activity of cathepsins are tightly regulated through several mechanisms:
- Transcriptional Regulation: Gene expression of cathepsins is controlled by transcription factors.
- Post-Translational Modifications: Cathepsins undergo modifications such as glycosylation, which affect their stability and activity .
- Endogenous Inhibitors: Proteins like stefins, cystatins, and serpins regulate cathepsin activity by inhibiting their proteolytic functions .
Applications
Cathepsins have significant applications in biomedical research, diagnostics, and therapeutics:
- Biomedical Research: They are studied for their roles in various diseases, including cancer and cardiovascular diseases .
- Diagnostic Tools: Differential expression of cathepsins can serve as biomarkers for disease progression .
- Therapeutic Strategies: Selective inhibitors of cathepsins are being developed as potential treatments for diseases .
Role in the Life Cycle
Cathepsins play vital roles throughout the life cycle, from development to aging and disease:
- Development: They are involved in tissue remodeling during embryogenesis and development .
- Aging: Cathepsin activity is linked to the degradation of cellular components, which is crucial for maintaining cellular homeostasis .
- Disease: Dysregulated cathepsin activity is associated with various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases .
