This recombinant human MYL12B protein (amino acids 1-172) is expressed in E. coli with a C-terminal 6×His tag, demonstrating high purity (>95% by SDS-PAGE) and low endotoxin levels (<1.0 EU/μg, LAL method). Functional validation via ELISA confirms its reactivity with anti-MYL9 antibody (CSB-RA015318MA1HU) (EC50: 19.290–28.646 ng/mL at 2 μg/mL immobilization), suggesting shared epitopes within the myosin light chain family. Provided as lyophilized powder, this recombinant MYL12B protein ensures stability and ease of use in biochemical assays. The His tag facilitates purification while preserving functional domains. This protein serves as a critical tool for investigating actomyosin dynamics, mechanotransduction pathways, and diseases associated with myosin light chain dysfunction.
The human MYL12B protein is a significant component of the myosin regulatory light chain family, playing a pivotal role in the regulation of non-muscle myosin II activity. Myosin light chains are crucial for muscle contractility as they modulate the ATPase activity of myosin motors, enabling muscle contractions and various forms of motility in non-muscle cells. Specifically, MYL12B, along with its counterparts MYL12A and MYL9, is implicated in processes such as cytokinesis and cell locomotion, highlighting its relevance to cellular dynamics during both normal and pathological conditions, including cancer progression [1].
Moreover, MYL12B's expression has been linked with various physiological and pathological states. For instance, during cardiac remodeling, MYL12B is down-regulated, with associated alterations in actomyosin proteins impacting the contractile function of cardiac tissues [2]. Additionally, the regulation and phosphorylation of MYL12B are critical for maintaining the stability of myosin II complexes and the structural integrity of cells, emphasizing its role in cellular mechanics and motility [3][4].
Notably, the dysregulation of MYL12B is associated with cancer, as elevated expression levels have been observed in cancerous tissues, pointing to its potential function as a prognostic biomarker for conditions such as pancreatic ductal adenocarcinoma [1][5]. In vascular smooth muscle cells, MYL12B is particularly important for contractility and remodeling, responding dynamically to various stimuli, suggesting its functional versatility [6].
References:
[1] O. Menyhárt, Á. Bartha, & B. Győrffy. Preserved correlation matrices pinpoint extracellular matrix organization as a critical factor in pancreatic ductal adenocarcinoma. F1000research, vol. 12, p. 418, 2023. https://doi.org/10.12688/f1000research.131414.1
[2] S. Nordmeyer, M. Kraus, et al. Disease- and sex-specific differences in patients with heart valve disease: a proteome study. Life Science Alliance, vol. 6, no. 3, p. e202201411, 2023. https://doi.org/10.26508/lsa.202201411
[3] K. Limbutara, A. Kelleher, C. Yang, V. Raghuram, & M. Knepper. Phosphorylation changes in response to kinase inhibitor h89 in pka-null cells. Scientific Reports, vol. 9, no. 1, 2019. https://doi.org/10.1038/s41598-019-39116-2
[4] I. Park, C. Han, et al. Myosin regulatory light chains are required to maintain the stability of myosin ii and cellular integrity. Biochemical Journal, vol. 434, no. 1, p. 171-180, 2011. https://doi.org/10.1042/bj20101473
[5] H. Li, Y. Han, et al. Combined mendelian randomization and quantitative proteomics analysis to study the influence of thyroid dysfunction on acute ischemic stroke. Medcomm – Future Medicine, vol. 3, no. 4, 2024. https://doi.org/10.1002/mef2.70002
[6] X. Hu, L. You, et al. Effects of β‑hydroxybutyric acid and ghrelin on the motility and inflammation of gastric antral smooth muscle cells involving the regulation of growth hormone secretagogue receptor. Molecular Medicine Reports, 2019. https://doi.org/10.3892/mmr.2019.10739
