MYL9 Mouse
Description
MYL9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-172 a.a) and having a molecular mass of 22.4kDa.
MYL9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
MYL9 is a regulatory light chain of myosin II, a motor protein involved in actin-based motility. The recombinant form of MYL9 from mice is typically expressed in Escherichia coli (E. coli) and purified to high levels of purity, often exceeding 90% . The protein consists of 172 amino acids and has a molecular mass of approximately 22.4 kDa . It is often tagged with a His-tag at the N-terminus to facilitate purification .
MYL9 is involved in the regulation of myosin ATPase activity, which is crucial for muscle contraction. It binds to the myosin heavy chain and modulates its interaction with actin filaments. This interaction is regulated by the phosphorylation of MYL9, which is mediated by myosin light chain kinase (MLCK). Phosphorylation of MYL9 enhances the ATPase activity of myosin, leading to increased muscle contraction and cellular motility.
The role of MYL9 extends beyond muscle contraction. It is involved in various cellular processes, including:
- Cytokinesis: MYL9 is essential for the final separation of daughter cells during cell division.
- Cell Migration: It plays a role in the movement of cells, which is crucial for wound healing and immune responses.
- Smooth Muscle Function: MYL9 is particularly important in smooth muscle cells, where it regulates contraction and relaxation.
Recombinant MYL9 is widely used in research to study muscle physiology, cell motility, and signal transduction pathways. It is also used in biochemical assays to investigate the regulation of myosin ATPase activity and the effects of phosphorylation on myosin function.
