Recombinant Proteins
Product List
MYBPC3 Human
Myosin Binding Protein C, Cardiac Human Recombinant
MYL1 Human
Myosin Light Chain 1 Human Recombinant
MYL12A Human
Myosin Light Chain 12A Human Recombinant
MYL12A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (1-171 a.a.) and having a molecular mass of 22.4kDa.
MYL12A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MYL12B Human
Myosin Light Chain 12B Human Recombinant
MYL12B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MYL2 Human
Myosin Light Chain 2 Human Recombinant
MYL4 Human
Myosin Light Chain 4 Human Recombinant
MYL4 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
MYL5 (1-173 a.a.) Human
Myosin Light Chain 5 (1-173 a.a.) Human Recombinant
MYL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-173 a.a.) and having a molecular mass of 22.1kDa.
MYL5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MYL5 Human
Myosin Light Chain 5 Human Recombinant
MYL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-132 a.a.) and having a molecular mass of 17.4kDa.
MYL5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MYL6 Human
Myosin Light Chain 6 Human Recombinant
MYL6 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 19.1kDa. The MYL6 is purified by proprietary chromatographic techniques.
MYL6B Human
Myosin Light Chain 6B Human Recombinant
The MYL6B is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Introduction
Myosin light chains (MLCs) are small polypeptide subunits of myosin, a motor protein involved in muscle contraction and various cellular processes. MLCs are classified into two main types: Essential or Alkali MLCs (MLC1 or ELC) and Regulatory MLCs (MLC2 or RLC) . Essential MLCs are crucial for the structural integrity of the myosin molecule, while regulatory MLCs play a role in modulating the activity of myosin through phosphorylation .
Key Biological Properties: MLCs belong to the EF-hand family of Ca²⁺-binding proteins and contain two Ca²⁺-binding EF-hand motifs . They are involved in force transduction and cross-bridge kinetics in muscle contraction .
Expression Patterns and Tissue Distribution: MLCs are expressed in various tissues, including striated muscle (skeletal and cardiac) and smooth muscle . Specific genes encode different MLC isoforms, such as MYL1, MYL3, MYL4, and MYL6 for MLC1, and MYL2, MYL5, MYL7, and MYL9 for MLC2 .
Primary Biological Functions: MLCs are essential for muscle contraction by stabilizing the myosin head and modulating its interaction with actin . They contribute to force production and the regulation of muscle contraction dynamics .
Role in Immune Responses and Pathogen Recognition: While MLCs are primarily known for their role in muscle contraction, they also play a part in cellular motility and immune responses by facilitating the movement of immune cells .
Mechanisms with Other Molecules and Cells: MLCs interact with the neck region of myosin heavy chains (MHCs), stabilizing the complex and enabling the motor protein’s function . Regulatory MLCs undergo phosphorylation, which induces conformational changes that modulate myosin activity .
Binding Partners and Downstream Signaling Cascades: MLCs bind to actin filaments and are involved in the ATP-dependent cyclic interactions that drive muscle contraction . The phosphorylation of regulatory MLCs by myosin light chain kinase (MLCK) is a key regulatory step .
Transcriptional Regulation: The expression of MLC genes is regulated by various transcription factors and signaling pathways that respond to developmental and physiological cues .
Post-Translational Modifications: Phosphorylation is the primary post-translational modification that regulates MLC activity. MLCK phosphorylates regulatory MLCs, enhancing their interaction with actin and promoting muscle contraction .
Biomedical Research: MLCs are studied extensively in muscle physiology and pathology, providing insights into muscle function and diseases .
Diagnostic Tools: Alterations in MLC expression or function can serve as biomarkers for muscle-related diseases, such as cardiomyopathies .
Therapeutic Strategies: Targeting MLC phosphorylation pathways holds potential for developing treatments for muscle disorders and improving muscle function .
Development: MLCs are crucial for muscle development and differentiation, with specific isoforms expressed at different developmental stages .
Aging and Disease: Changes in MLC expression and function are associated with age-related muscle decline and various muscle diseases, including hypertrophic and dilated cardiomyopathy .
