Date published: 2026-2-4

1-800-457-3801

SCBT Portrait Logo
Seach Input

cathepsin C Substrates

Santa Cruz Biotechnology now offers a broad range of cathepsin C Substrates for use in various applications. Cathepsin C substrates are essential tools in the study of cathepsin C, a lysosomal cysteine protease that plays a critical role in immune function, particularly in the activation of serine proteases in immune cells like neutrophils and cytotoxic T lymphocytes. Cathepsin C, also known as dipeptidyl peptidase I, is involved in the removal of dipeptides from the N-terminus of protein substrates, which is a crucial step in the maturation and activation of several proteases that are important for immune responses, including granzymes and cathepsins G and H. By utilizing cathepsin C substrates, researchers can specifically monitor the activity of this enzyme, providing insights into its functional role in both normal physiology and in the context of immune-related diseases. These substrates are widely used in research to understand the biochemical pathways regulated by cathepsin C, as well as in high-throughput screening assays aimed at identifying novel modulators of its activity. Understanding the activity of cathepsin C through these substrates is also significant in studies of diseases such as chronic inflammatory conditions, where dysregulation of this enzyme can lead to pathological outcomes. The use of cathepsin C substrates is thus crucial for advancing research in immunology, cell biology, and pathology, offering a deeper understanding of how proteolytic processing by cathepsin C influences cellular processes and immune functions. View detailed information on our available cathepsin C Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Gly-Phe β-naphthylamide

21438-66-4sc-252858
sc-252858A
100 mg
1 g
$84.00
$686.00
53
(2)

Gly-Phe β-naphthylamide acts as a selective inhibitor of cathepsin C, characterized by its unique ability to form stable interactions with the enzyme's catalytic triad. The compound's β-naphthyl moiety enhances hydrophobic stacking, while the Gly-Phe dipeptide promotes specific electrostatic interactions. This results in a conformational shift in the enzyme, effectively modulating its activity. Kinetic studies indicate a competitive inhibition mechanism, underscoring its specificity in proteolytic regulation.