CTSL Mouse

Cathepsin-L Mouse Recombinant

CTSL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (18-334a.a.) and having a molecular mass of 36.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
CTSL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30670
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

CTSS Human

Cathepsin-S Human Recombinant

CTSS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (17-331) and having a molecular mass of 38.1kDa. CTSS is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. 
Shipped with Ice Packs
Cat. No.
BT30714
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

CTSS Mouse

Cathepsin-S Mouse Recombinant

CTSS Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 325 amino acids (24-340 a.a.) and having a molecular mass of 36.9kDa.
CTSS is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30748
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

CTSW Human

Cathepsin-W Human Recombinant

CTSW Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (22-376) and having a molecular mass of 42.0 kDa. CTSW is fused to a 23 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT30768
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

CTSZ Human

Cathepsin-Z Human Recombinant

CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.
CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30801
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

CTSZ Human, Sf9

Cathepsin-Z Human Recombinant, Sf9

CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
 
Shipped with Ice Packs
Cat. No.
BT30810
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered clear solution.

CTSZ Mouse

Cathepsin-Z Mouse Recombinant

CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (23-306a.a.) and having a molecular mass of 32.8kDa. 
(Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30829
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.

CTSZ Mouse, Active

Cathepsin-Z, Active Mouse Recombinant

CTSZ Mouse Recombinant produced in Baculovirus is a single, glycosylated, polypeptide chain containing 292 amino acids (23-306 aa) and having a molecular mass of 32.8kDa.
CTSZ is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT30854
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.
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

Cathepsins exhibit a variety of biological properties, including their expression patterns and tissue distribution. They are most abundant in lysosomal compartments, where they function optimally at acidic pH levels . Different cathepsins are expressed in various tissues:

  • Cathepsin K: Found in osteoclasts and epithelial cells.
  • Cathepsin S, E, and W: Predominantly expressed in immune cells .
Biological Functions

Cathepsins are involved in several primary biological functions:

  • Protein Degradation: They break down proteins into peptides and amino acids.
  • Immune Responses: Cathepsins play a role in antigen processing and presentation, which is crucial for immune responses .
  • Pathogen Recognition: They are involved in the degradation of pathogens within lysosomes .
Modes of Action

Cathepsins interact with other molecules and cells through various mechanisms:

  • Binding Partners: They bind to specific substrates and inhibitors.
  • Downstream Signaling Cascades: Cathepsins can activate or inhibit signaling pathways that regulate cell survival, apoptosis, and inflammation .
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 .
© Copyright 2024 Thebiotek. All Rights Reserved.