Datasheet

Biological Description

Specificity	Anti-Phospho-Myosin Light Chain 2 (Thr18/Ser19) Rabbit Antibody [C13P19] detects endogenous levels of myosin light chain 2 protein only when phosphorylated at Thr18 and Ser19.
Background	Phospho-Myosin Light Chain 2 (Thr18/Ser19) (MLC2) refers to the regulatory light chain of myosin II, which is phosphorylated at threonine 18 (Thr18) and serine 19 (Ser19) residues by myosin light chain kinase (MLCK) and other kinases. Structurally, MLC2 is composed of a single polypeptide associated with the myosin heavy chain, and its N-terminal region contains the key phosphorylation sites that regulate myosin motor activity. MLC2 is widely expressed in smooth muscle, nonmuscle cells, and platelets, where it plays a central role in cytoskeletal dynamics, contractility, and motile processes. Phosphorylation at Ser19, and to a lesser extent Thr18, activates myosin II by enhancing its ATPase activity and promoting filament assembly, leading to actin-myosin interactions essential for cell contraction, migration, and shape changes. Distinct signaling pathways differentially regulate these phosphorylation sites: Ser19 is rapidly phosphorylated downstream of Ca²⁺/MLCK-dependent pathways, driving immediate contractile responses, whereas Thr18 phosphorylation is slower and often linked to Rho kinase–dependent pathways, fine-tuning contractility. Together, Thr18/Ser19 phosphorylation provides a graded mechanism to control myosin II activity, enabling precise regulation of actomyosin-mediated processes such as platelet shape change, stress fiber formation, and cellular motility.

Specificity

Anti-Phospho-Myosin Light Chain 2 (Thr18/Ser19) Rabbit Antibody [C13P19] detects endogenous levels of myosin light chain 2 protein only when phosphorylated at Thr18 and Ser19.

Background

Phospho-Myosin Light Chain 2 (Thr18/Ser19) (MLC2) refers to the regulatory light chain of myosin II, which is phosphorylated at threonine 18 (Thr18) and serine 19 (Ser19) residues by myosin light chain kinase (MLCK) and other kinases. Structurally, MLC2 is composed of a single polypeptide associated with the myosin heavy chain, and its N-terminal region contains the key phosphorylation sites that regulate myosin motor activity. MLC2 is widely expressed in smooth muscle, nonmuscle cells, and platelets, where it plays a central role in cytoskeletal dynamics, contractility, and motile processes. Phosphorylation at Ser19, and to a lesser extent Thr18, activates myosin II by enhancing its ATPase activity and promoting filament assembly, leading to actin-myosin interactions essential for cell contraction, migration, and shape changes. Distinct signaling pathways differentially regulate these phosphorylation sites: Ser19 is rapidly phosphorylated downstream of Ca²⁺/MLCK-dependent pathways, driving immediate contractile responses, whereas Thr18 phosphorylation is slower and often linked to Rho kinase–dependent pathways, fine-tuning contractility. Together, Thr18/Ser19 phosphorylation provides a graded mechanism to control myosin II activity, enabling precise regulation of actomyosin-mediated processes such as platelet shape change, stress fiber formation, and cellular motility.

Usage Information

Application

WB, IF

Dilution

WB	IF
1:1000	1:400 - 1:800

Reactivity

Human, Mouse, Rat

Source

Rabbit

MW

18 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/20670370/
https://pubmed.ncbi.nlm.nih.gov/17928407/

Anti-Phospho-Myosin Light Chain 2 (Thr18/Ser19) Rabbit Antibody [C13P19]

Biological Description

Usage Information

References

Application Data