Recombinant Proteins

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MYL12B Human

Myosin Light Chain 12B Human Recombinant

Recombinantly produced in E. coli, MYL12B Human Recombinant is a single polypeptide chain consisting of 196 amino acids (residues 1-172). It possesses a molecular weight of 22.3 kDa. For purification purposes, MYL12B is tagged with a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15301
Source
E.coli.
Appearance
A clear, sterile solution.

MYL2 Human

Myosin Light Chain 2 Human Recombinant

Recombinant human MYL2 protein was produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of 186 amino acids (residues 1-166). It has a molecular weight of 20.9 kDa. A 20 amino acid His-tag is fused to the N-terminus to facilitate purification. The protein was purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15381
Source
Escherichia Coli.
Appearance
A clear, colorless and sterile solution.

MYL4 Human

Myosin Light Chain 4 Human Recombinant

Recombinant MYL4, specifically the human variant, is produced in E. coli bacteria. This process yields a single, non-glycosylated polypeptide chain consisting of 205 amino acids (specifically amino acids 1 through 197). The resulting protein has a molecular weight of 22.6 kDa. For purification and analytical purposes, an 8-amino acid His-tag is attached to the C-terminus of the MYL4 protein. Purification is then achieved using specialized chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15457
Source
E.coli.
Appearance
The purified MYL4 solution is sterile-filtered and appears colorless.

MYBPC3 Human

Myosin Binding Protein C, Cardiac Human Recombinant

This product is a lab-created version of a small part of the human MYBPC3 protein. It's made in E. coli bacteria and comes as a dry powder. This powder represents a single chain of 281 building blocks of the protein, with a small tag added for identification. It's important to note that this product is not meant for direct use in humans.
Shipped with Ice Packs
Cat. No.
BT15103
Source
Escherichia Coli.
Appearance
White powder that has been freeze-dried and filtered.

MYL6 Human

Myosin Light Chain 6 Human Recombinant

Recombinant human MYL6, with a 20 amino acid His tag added at the N-terminus, is produced in E. coli as a single, non-glycosylated polypeptide chain. This protein consists of 171 amino acids (specifically, amino acids 1-151) and has a molecular weight of 19.1 kDa. Purification of MYL6 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15681
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

MYL6B Human

Myosin Light Chain 6B Human Recombinant

Recombinantly produced in E. coli, MYL6B Human Recombinant is a non-glycosylated polypeptide chain that is devoid of any glycosylation modifications. It encompasses 231 amino acids (residues 1-208) and possesses a molecular weight of 25.2 kDa. For purification purposes, a 23-amino acid His-Tag is fused to the N-terminus of the MYL6B protein, facilitating its isolation through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15732
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

MYL1 Human

Myosin Light Chain 1 Human Recombinant

Recombinant Human Ventricular Myosin Light Chain-1 (MYL1) protein, with a molecular weight of 25 kDa, is fused to a 7 amino acid sequence at the N-terminus. The MYL1 protein was purified through affinity chromatography using an anti-MYL1 monoclonal antibody 39-15 column.
Shipped with Ice Packs
Cat. No.
BT15175
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

MYL12A Human

Myosin Light Chain 12A Human Recombinant

Recombinant human MYL12A, expressed in E. coli bacteria, is a single polypeptide chain that lacks glycosylation. It comprises 195 amino acids (specifically, amino acids 1 to 171) and has a molecular weight of 22.4 kDa. The protein includes a 24 amino acid His-tag at its N-terminus to aid in purification, which is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15221
Source
Escherichia Coli.
Appearance
A clear and sterile solution.

MYL7 Human

Myosin Light Chain 7 Human Recombinant

Recombinantly produced in E. coli, MYL7 Human is a single polypeptide chain consisting of 199 amino acids (residues 1-175) and possesses a molecular mass of 22.0 kDa. The protein is fused to a 24 amino acid His-tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15819
Source
E.coli.
Appearance
A colorless solution that has undergone sterile filtration.

MYL9 Human

Myosin Light Chain 9 Human Recombinant

Recombinant human MYL9, fused with a 20 amino acid His tag at the N-terminus, is produced in E. coli. This yields a single, non-glycosylated polypeptide chain containing 192 amino acids (residues 1-172) with a molecular weight of 21.9 kDa. The purification of MYL9 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15920
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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 .

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