Date published: 2026-3-10

1-800-457-3801

SCBT Portrait Logo
Seach Input

MYLK Substrates

Santa Cruz Biotechnology now offers a broad range of MYLK Substrates for use in various applications. Myosin light chain kinase (MYLK) is an enzyme that plays a crucial role in regulating muscle contraction and cell motility through the phosphorylation of myosin light chains. This kinase is essential for the function of smooth, cardiac, and skeletal muscles, as well as for non-muscle cells involved in various physiological processes such as cell division, migration, and maintaining the integrity of the endothelial barrier. MYLK Substrates are indispensable tools in scientific research, allowing researchers to investigate the specific activities and regulatory mechanisms of MYLK in different cellular contexts. By using these substrates, scientists can explore how MYLK-mediated phosphorylation affects myosin interactions with actin filaments, leading to changes in muscle contraction and cell movement. These substrates are widely used in studies focused on understanding the molecular mechanisms underlying muscle physiology, as well as in research exploring the role of MYLK in pathological conditions such as hypertension, asthma, and certain forms of cancer where MYLK signaling may be dysregulated. Additionally, MYLK Substrates are valuable in the development of potential therapeutic strategies aimed at modulating MYLK activity to treat diseases associated with abnormal muscle contraction and cell motility. The availability of these substrates has significantly advanced research in cell biology, physiology, and biochemistry, providing critical insights into the complex regulatory networks that control muscle function and cellular dynamics. View detailed information on our available MYLK Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

MYLK/MYLK2 Substrate

sc-3043
1 mg
$96.00
1
(0)

MYLK/MYLK2 Substrate acts as a potent activator of myosin light chain kinase, characterized by its ability to stabilize enzyme-substrate complexes through electrostatic interactions. This substrate promotes a unique allosteric modulation, enhancing the enzyme's catalytic efficiency. Its structural conformation allows for optimal alignment with the active site, facilitating rapid phosphorylation events. Furthermore, its dynamic solvation properties enable effective interaction with diverse cellular components, influencing regulatory mechanisms.