Date published: 2026-5-27

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TPPII Substrates

Santa Cruz Biotechnology now offers a broad range of TPPII Substrates for use in various applications. TPPII Substrates, which are peptides specifically designed to be hydrolyzed by the enzyme tripeptidyl-peptidase II (TPPII), are crucial tools in biochemical and cellular research. TPPII is a protease involved in the degradation of proteins within cells, playing a key role in various cellular processes, including protein quality control, antigen processing, and the regulation of peptide hormone activity. By providing a diverse selection of TPPII Substrates, researchers can explore the enzyme's function and regulation in different contexts, such as studying its role in protein turnover and degradation pathways. The availability of these substrates allows for precise investigations into enzyme kinetics, substrate specificity, and the identification of potential inhibitors or modulators of TPPII activity. This category of chemicals is particularly valuable in explaining the mechanisms of proteostasis and the intricate balance of protein synthesis and degradation in cells. Santa Cruz Biotechnology's extensive range of TPPII Substrates supports advanced research in molecular biology, biochemistry, and cell biology, offering scientists the necessary tools to deepen their understanding of protein dynamics. View detailed information on our available TPPII Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

L-Alanyl-L-alanyl-L-phenylalanine 7-amido-4-methylcoumarin

62037-41-6sc-218626
25 mg
$171.00
(1)

L-Alanyl-L-alanyl-L-phenylalanine 7-amido-4-methylcoumarin serves as a substrate for TPPII, characterized by its unique ability to engage in specific non-covalent interactions with enzyme active sites. This compound's structural features allow for enhanced substrate specificity, influencing the rate of enzymatic reactions. Its fluorescence properties enable real-time monitoring of enzymatic activity, while its conformational flexibility aids in optimizing binding affinity and reaction dynamics within complex biochemical environments.