Date published: 2026-1-9

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TGase Substrates

Santa Cruz Biotechnology now offers a broad range of TGase substrates for use in various applications. TGase substrates are essential in the study of enzyme activity and protein cross-linking processes. These substrates are particularly valuable in the field of biochemistry and molecular biology, where they serve as crucial tools for investigating the role of transglutaminase enzymes in cellular functions. TGase enzymes catalyze the formation of covalent bonds between proteins, influencing protein structure, stability, and function. This makes TGase substrates indispensable in the study of protein modification, interaction, and assembly. Researchers utilize these substrates to explore the mechanisms underlying protein aggregation, a phenomenon relevant in understanding the biochemical pathways of numerous cellular processes. Furthermore, TGase substrates are employed in the development of bio-materials and in the food industry for modifying protein properties. Their ability to mimic natural substrates allows for detailed kinetic and mechanistic studies, thereby advancing our knowledge of enzyme specificity and regulation. As tools in experimental setups, TGase substrates contribute to the creation of more accurate models for studying complex biological systems. View detailed information on our available TGase substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

α-Endorphin

59004-96-5sc-391797
sc-391797A
1 mg
5 mg
$77.00
$175.00
(0)

α-Endorphin acts as a significant TGAse, characterized by its ability to engage in specific molecular interactions, including hydrophobic effects and van der Waals forces. This peptide exhibits unique conformational flexibility, allowing it to adopt various structural states that influence its reactivity. Its interactions with receptor sites are governed by intricate kinetics, enabling selective binding and modulation of biological pathways, which underscores its role in complex biochemical networks.