Recombinant Human Myosin Regulatory Light Chain 2, Ventricular/Cardiac Muscle Isoform (MYL2) Protein (His)

Name: Recombinant Human Myosin Regulatory Light Chain 2, Ventricular/Cardiac Muscle Isoform (MYL2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08332P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Myosin Regulatory Light Chain 2, Ventricular/Cardiac Muscle Isoform (MYL2) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P10916
Target Symbol	MYL2
Synonyms	Cardiac myosin light chain-2; Cardiac ventricular myosin light chain 2; CMH10; MLC 2v ; MLC-2; MLC-2v; MLC2; MLRV_HUMAN; MYL 2; MYL2; Myosin light chain 2 regulatory cardiac slow; Myosin light polypeptide 2 regulatory cardiac slow; Myosin regulatory light chain 2; Myosin regulatory light chain 2 ventricular/cardiac muscle isoform; Regulatory light chain of myosin; RLC of myosin; Slow cardiac myosin regulatory light chain 2; ventricular/cardiac muscle isoform
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KRAGGANSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITHGEE
Expression Range	8-164aa
Protein Length	Partial
Mol. Weight	21.8kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Contractile protein that plays a role in heart development and function. Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force. During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly.
Subcellular Location	Cytoplasm, myofibril, sarcomere, A band.
Database References	HGNC: 7583 OMIM: 160781 KEGG: hsa:4633 STRING: 9606.ENSP00000228841 UniGene: PMID: 29463717 These results indicate shear stress induced vascular smooth muscle cell contraction was mediated by cell surface glycocalyx via a ROCK-MLC phosphatase (MLCP) pathway, providing evidence of the glycocalyx mechanotransduction in myogenic response. PMID: 28191820 The results show that the MYL2 mutation c.64G > A on its own is incapable of triggering clinical HCM in most carriers. However, the presence of an additional risk factor for hypertrophy, particularly hypertension, adds to the development of HCM. PMID: 26497160 Our study provides the first evidence that miR-223 can regulate pulmonary artery smooth muscle cells proliferation, migration, and actomyosin reorganization through its novel targets, RhoB and MLC2, resulting in vascular remodeling and the development of pulmonary arterial hypertension. PMID: 27121468 NKX2-5 and MLC2v double-positive cells possess ventricular-like properties. The results demonstrate that the NKX2-5(eGFP/w) and MLC2v(mCherry/w) hPSCs provide a powerful model system to capture region-specific cardiac differentiation from early to late stages. Our study would facilitate subtype-specific cardiac development and functional analysis using the hPSC-derived sources. PMID: 29175323 This exome-wide association study indicated that C12orf51 rs11066280, MYL2 rs12229654, and ALDH2 rs671 polymorphisms are linked to blood Pb levels in the Korean population. PMID: 28212632 Mutation in myosin regulatory light chain gene is associated with defective myosin motor function that ultimately result in pathological hypertrophic remodeling. PMID: 28467684 Lipolysis-stimulated lipoprotein receptors (LSRs) localized to bicellular junctions in association with myosin regulatory light chain 2 (MRLC2) at low cell densities and to tricellular contacts when myosin phosphatase target subunit 1 (MYPT1) localized to the bicellular regions. PMID: 28493278 Structural dynamics-based approach reveals that the E56G mutation in human ventricular essential light chain affects the structure of the actin-myosin complex in the presence of ATP. The mutation increases the population in the S structural state (increasing the duty ratio), and changes the structure of the W state, so that it more closely resembles the S state. PMID: 28700929 Two siblings with hypertrophic cardiomyopathy had the pathogenic variant p.Ala13Thr variant in MYL2. PMID: 28223422 the MYL2 gene on chromosome 12 is associated with serum HDL-C levels in Korean men. The association was much stronger in male obese subjects and smokers than that in leaner nonsmoking male subjects. PMID: 26763873 FLNb enhances invasion of cancer cells through phosphorylation of MRLC and FAK. PMID: 25925610 Ostf1b could constitutively activate the Rho kinase 1 (ROCK1) and myosin light chain 2 (MLC2) signalling pathway that promotes cell migration, epithelial mesenchymal transition (EMT) and cytoskeletal dynamics through stress fibre formation. PMID: 23732111 Myosin regulatory light chain phosphorylation enhances cardiac beta-myosin in vitro motility under load. PMID: 26116789 This review focuses on the regulatory functions of MLC-2 in the embryonic and adult heart, with an emphasis on phosphorylation-driven actions of MLC-2v in adult cardiac muscle. PMID: 26074085 Data suggest a mutation in MYL2 (amino acid substitution D94A; novel mutation in familial dilated cardiomyopathy) does affect conformation (reduced alpha-helical content) and function (reduced binding of myosin heavy chain; increased ATPase) of MYL2. PMID: 25825243 Four novel body mass index-associated loci near the KCNQ1(rs2237892), ALDH2/MYL2 (rs671, rs12229654), ITIH4 (rs2535633) and NT5C2 (rs11191580) genes are identified in East Asian-ancestry populations. PMID: 24861553 Results suggest that Aurora B, but not Rho/MLCK (myosin-light-chain kinase) signaling, is essential for the localization of 2P-MRLC (myosin regulatory light chains) to the midzone in dividing HeLa cells. PMID: 23951055 an interplay between phosphorylation and glycosylation of MLC2, which might be involved in the development of muscle atrophy and associated changes PMID: 24184274 Newly implicated variants (MYL2, C12orf51 and OAS1) were found to be significantly associated with 1-h plasma glucose as predisposing risk factors for type 2 diabetes. PMID: 23575436 study concludes the mutations in the last exon of MYL2 are responsible for a novel autosomal recessive lethal myosinopathy due to defects changing the C-terminal tail of the ventricular form of the myosin regulatory light chain PMID: 23365102 NDRG1 inhibited an important regulatory pathway mediated by ROCK1/pMLC2 pathway that modulates stress fiber assembly. PMID: 23188716 AMPK mediates spindle pole-associated pMRLC(ser19) to control spindle orientation via regulation of actin cortex-astral microtubule attachments PMID: 22688514 MLC2 isoforms localisation is dependent on cell cycle in HeLa cells. PMID: 22425609 results suggest that the A13T mutation triggers a hypertrophic response through changes in cardiac sarcomere organization and myosin cross-bridge function leading to abnormal remodelling of the heart. PMID: 22091967 These data demonstrate that smMLCK is a specific and efficient kinase for the in vitro phosphorylation of MYL2, cardiac, and smooth muscle myosin. PMID: 22120626 This is the first report of mutations in TPM1, MY L3, and MYL2 associated with primary, non-hypertrophied restrictive cardiomyopathy. PMID: 21823217 MYL2 was down-expressed in heart failure tissues, and findings suggested that MYL2 may play a role in the development and progression of chronic heart failure. PMID: 21259275 Oxidative stress related to asphyxia induces nitration of cardiac MLC2 protein and thus increases its degradation. This and a large decrease in MLC2 phosphorylation contribute to the development of systolic dysfunction. PMID: 20386496 Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 have functional implications in platelets PMID: 20670370 mutations in familial hypertrophic cardiomyopathy: phenotypic presentation and frequency in Danish and South African populations PMID: 11748309 diphosphorylated MRLC and Rho-kinase accumulated and colocalized at the contractile ring and the midbody in dividing cells PMID: 12185584 MLC2 phosphorylation is regulated by both ROCK and MLC kinase and plays an important role in platelet biogenesis by controlling proplatelet formation and fragmentation. PMID: 17244674 DLC1 negatively regulates Rho/ROCK/MLC2 PMID: 18648664 Following down-regulation of MR-1, the phosphorylations of MLC2, focal adhesion kinase (FAK), and Akt were dramatically decreased PMID: 18948272 Profound cellular changes observed in Tg-D166V myocardium when placed in vivo could trigger a series of pathological responses and result in poor prognosis for D166V-positive patients. PMID: 18987303 These results indicate that diphosphorylation of regulatory light chain of myosin IIA by Rho-kinase in lamella is responsible for the cell to spread properly. PMID: 19254691 Data show that VE-cadherin signals to Rho-kinase-dependent myosin light-chain 2 phosphorylation, leading to actomyosin contractility, which regulates the distribution of VE-cadherin at cell-cell junctions and sprouting. PMID: 19345098

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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