MYL2
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Official Full Name
Myosin regulatory light chain 2
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Overview
Myosins comprise a family of ATP-dependent motor proteins and are best known for their role in muscle contraction and their involvement in a wide range of other eukaryotic motility processes. They are responsible for actin-based motility. The term was originally used to describe a group of similar ATPases found in striated and smooth muscle cells. Following the discovery by Pollard and Korn of enzymes with myosin-like function in Acanthamoeba castellanii, a large number of divergent myosin genes have been discovered throughout eukaryotes. Thus, although myosin was originally thought to be restricted to muscle cells (hence, "myo"), there is no single "myosin" but rather a huge superfamily of genes whose protein products share the basic properties of actin binding, ATP hydrolysis (ATPase enzyme activity), and force transduction. Virtually all eukaryotic cells contain myosin isoforms. Some isoforms have specialized functions in certain cell types (such as muscle), while other isoforms are ubiquitous. The structure and function of myosin is strongly conserved across species, to the extent that rabbit muscle myosin II will bind to actin from an amoeba. -
Synonyms
Myosin regulatory light chain 2; MYL2;
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- Interacting Protein
- MYL2 Related Articles
What is MYL2 protein?
MYL2 (myosin light chain 2) gene is a protein coding gene which situated on the long arm of chromosome 12 at locus 12q24. Myosin light chain 2 (MYL2) encodes the regulatory light chain associated with cardiac myosin beta heavy chain. It is an important protein involved in the regulation of myosin ATPase activity in smooth muscle and Ca+ triggers the phosphorylation of regulatory light chain that in turn triggers contraction. The MYL2 protein is consisted of 166 amino acids and its molecular mass is approximately 18.8 kDa.
What is the function of MYL2 protein?
MYL2 is a muscle-specific protein, its main function is to bind with myosin, form myosin complex, participate in myosin conformational change and intermyotome sliding, thereby regulating muscle contraction process. In addition, it plays an important role in muscle development and growth by participating in the proliferation and differentiation of muscle cells. It is also an ontractile protein that plays a role in heart development and function.
MYL2 Related Signaling Pathway
MYL2 can bind to calcium ions and participate in the regulation of calcium signaling pathways, regulating muscle contraction by binding Ca2+ ions and ATP. In addition, MYL2 can affect the occurrence and development of inflammatory response by regulating the expression and activity of inflammatory factors.
MYL2 Related Diseases
The mutated or mutated MYL2 gene is linked to a number of muscle and cardiovascular diseases, such as hypertrophic cardiomyopathy, congenital heart disease and arrhythmias. This suggests that MYL2 plays an important role in cardiac function and structural maintenance.
Fig1. Hypertrophic cardiomyopathy (HCM) is caused by transcriptomic defects in certain proteins of the sarcomere as a result of specific genomic alterations on thick and thin filaments and Z-disks. (Marilena Melas, 2022)
Bioapplications of MYL2
In terms of scientific research applications, antibodies against MYL2 are widely used in a variety of scientific research fields, including Western Blot, immunocytochemistry, immunohistochemistry, ELISA and flow cytometry. In addition, researchers are conducting in-depth exploration of the relationship between MYL2 gene and myocardial diseases to explore therapeutic targets.
High Purity
Fig1. SDS-PAGE (MYL2-5808H) (PROTOCOL for western blot)
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Fig2. SDS-PAGE (MYL2-4647H) (PROTOCOL for western blot)
Case Study 1: Bo Zhao, 2023
Fig1. Protein expression levels of Myh7, Atp1a3, Myl2, and Myl3 detected by western blotting.
Case Study 2: Pengcheng Pan, 2023
Fig2. The plasmid was transfected into C2C12 cells. (a1–c1), cells were observed under a fluorescence microscope at 10×; (a2–c2), cells observed under an optical microscope at 10×. (a1,a2), cells transfected with pEGFP-N1; (b1,b2), cells transfected with pEGFP-N1-MYL2; (c1,c2), blank control group.
Fig1. Overview of the mechanisms of cardiotoxicity caused by PS-MP. (Yue Zhou, 2023)
Fig2. Schematic representation of the CaMKII-mediated signaling pathways that regulate expression of downstream genes during muscle adaptation to loading, and which are defective in C3KO muscles. (Jian Liu, 2020)
MYL2 involved in several pathways and played different roles in them. We selected most pathways MYL2 participated on our site, such as Cardiac muscle contraction, Adrenergic signaling in cardiomyocytes, Focal adhesion, which may be useful for your reference. Also, other proteins which involved in the same pathway with MYL2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Cardiac muscle contraction | COX7A3;CACNA1SB;MYL3;TNNI3;CACNG2A;TPM4A;UQCRB;ATP1A1B;TMEM8C |
Adrenergic signaling in cardiomyocytes | VMHCL;GNAS;CACNA1D;ADCY1A;NETO2;ATP2B2;TNNT2;PPP2R2BB;GNAIA |
Focal adhesion | VCLA;MYL9;VWF;ITGA1;FYN;RHOAC;MYL12A;MAPK6;MAPK1 |
Tight junction | MPP5;EXOC4;SRC;PARD6B;ZAK;INADL;HCLS1;EPB41;ACTN3A |
Leukocyte transendothelial migration | MAPK11;ROCK2;OCLN;NIPAL1;PRKCG;CLDN4;CLDN7;ITGAL;CTNNA3 |
Regulation of actin cytoskeleton | PIP5K1C;RAC2;ABI2A;PIP5K2;PIK3R3A;ARHGEF7;ITGA6;FGF8A;VAV2 |
Hypertrophic cardiomyopathy (HCM) | PRKAG3;TTN;CACNA2D1;LMNA;PRKAG1;ITGA3;DES;EMD;MYL3 |
Dilated cardiomyopathy | TNF;TGFB2;CACNA2D2;PLN;DAG1;TTN;MYH7;LMNA;ITGA3 |
MYL2 has several biochemical functions, for example, actin monomer binding, calcium ion binding, myosin heavy chain binding. Some of the functions are cooperated with other proteins, some of the functions could acted by MYL2 itself. We selected most functions MYL2 had, and list some proteins which have the same functions with MYL2. You can find most of the proteins on our site.
Function | Related Protein |
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actin monomer binding | TWF2;MYL4;ABL2;TMSB15B;ABL1;PKNOX2;COBLL1;MKL1B;NOS3 |
calcium ion binding | CALB2A;LRP2;PLS3;SYT17;Amy1;PCDH2G12;PCDH2AB2;STIM1;HPGDS |
myosin heavy chain binding | MYL2;MYL9;PDLIM2;AMPD1;MYL12B;MYBPC3;CORO1A |
protein binding | PSIP1;KATNBL1;CHD1;RNF185;RUNX3;CCDC28B;GNAI2;RAB35;THRAP3 |
structural constituent of muscle | TTN;MYBPC3;MYL3;DAG1;PLEC;MYBPC2;ACTN2;ASPH;MYBPC1 |
MYL2 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MYL2 here. Most of them are supplied by our site. Hope this information will be useful for your research of MYL2.
USP6; GJB5; LRSAM1; NHP2
- Q&As
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Q&As (5)
Ask a questionStudies suggest that MYL2 expression levels may vary with age and gender, which could have implications for understanding cardiac health across different demographics.
Elevated MYL2 levels may be indicative of a poorer prognosis in certain cardiac conditions, providing valuable information for treatment planning.
Understanding the genetic variations in MYL2 allows for personalized treatment strategies tailored to an individual's specific cardiac profile.
Dysregulation of MYL2 is implicated in hypertrophic cardiomyopathy, contributing to our understanding of the molecular pathways leading to cardiac hypertrophy.
Analyzing MYL2 variants and expression levels can help identify individuals at a higher risk of developing cardiac disorders, allowing for proactive management.
Customer Reviews (3)
Write a reviewThe MYL2 Protein comes highly recommended for its exceptional performance, particularly in ELISA assays.
This protein has proven to be of great utility in protein electron microscopy structure analysis.
Researchers utilizing the MYL2 Protein can rely on its robust and reproducible performance in a variety of experimental settings.
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