CTSS Human

Cathepsin-S Human Recombinant

Recombinant human CTSS, expressed in E.coli, is a non-glycosylated polypeptide chain consisting of 336 amino acids (residues 17-331). It has a molecular weight of 38.1 kDa. The protein includes a 21 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30714
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution that has been filtered.

CTSS Mouse

Cathepsin-S Mouse Recombinant

Recombinant Mouse CTSS, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain containing 325 amino acids (residues 24-340). It has a molecular weight of 36.9 kDa. The protein includes an 8-amino acid His tag at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30748
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CTSW Human

Cathepsin-W Human Recombinant

Recombinant human CTSW, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 42.0 kDa. It comprises 378 amino acids (residues 22-376) and includes a 23 amino acid His-tag fused at the N-terminus.
Shipped with Ice Packs
Cat. No.
BT30768
Source
Escherichia Coli.
Appearance
A clear, sterile solution that has been filtered.

CTSZ Human

Cathepsin-Z Human Recombinant

Recombinant human CTSZ, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 265 amino acids (residues 62-303). It has a molecular weight of 29.5 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30801
Source
Escherichia Coli.
Appearance
Sterile, colorless solution, filtered for clarity.

CTSZ Human, Sf9

Cathepsin-Z Human Recombinant, Sf9

This part details the characteristics of the CTSZ protein produced in Sf9 Baculovirus cells, encompassing its structure, molecular weight, tag, and purification method.
 
Shipped with Ice Packs
Cat. No.
BT30810
Source

Sf9, Baculovirus cells.

Appearance
This describes the visual appearance of the supplied CTSZ protein solution after sterile filtration.

CTSZ Mouse

Cathepsin-Z Mouse Recombinant

CTSZ, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 292 amino acids (23-306a.a.) with a molecular mass of 32.8 kDa. On SDS-PAGE, the molecular size appears approximately between 28-40 kDa. CTSZ 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.
BT30829
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.

CTSZ Mouse, Active

Cathepsin-Z, Active Mouse Recombinant

Recombinant Mouse CTSZ, produced in Baculovirus, is a single, glycosylated polypeptide chain consisting of 292 amino acids (23-306 aa). It has a molecular weight of 32.8 kDa. The CTSZ protein is fused to an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT30854
Source

Sf9, Baculovirus cells.

Appearance
Clear, colorless solution, sterile filtered.

CTSC Mouse

Cathepsin-C Mouse Recombinant

Recombinant CTSC protein derived from mouse has been produced in HEK293 cells. This protein is a single polypeptide chain consisting of 444 amino acids (amino acids 25-462), resulting in a molecular weight of 50.5 kDa. A 6-amino acid Histidine tag is present at the C-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT30432
Source

HEK293 cells.

Appearance
Clear, sterile solution after filtration.

CTSF Human, Sf9

Cathepsin-F Human Recombinant, Sf9

Produced in Sf9 Baculovirus cells, CTSF is a single, glycosylated polypeptide chain with a molecular weight of 52.5kDa. It comprises 474 amino acids (20-484.a.a). The protein is expressed with a 6 amino acid His tag at the C-Terminus and purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT30605
Source

Sf9, Baculovirus cells.

Appearance

Sterile filtered, colorless solution.

CTSL Human

Cathepsin-L Human Recombinant

Recombinant human CTSL, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 339 amino acids (residues 18-333). It has a molecular weight of 38.3 kDa. The CTSL protein is fused to a 23-amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30630
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered 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 .
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