MYL2 Antibody, Biotin conjugated

Code CSB-PA10059D0Rb
Size US$166
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) MYL2 Polyclonal antibody
Uniprot No.
Target Names
MYL2
Alternative Names
Cardiac myosin light chain-2 antibody; Cardiac ventricular myosin light chain 2 antibody; CMH10 antibody; MLC 2v antibody; MLC-2 antibody; MLC-2v antibody; MLC2 antibody; MLRV_HUMAN antibody; MYL 2 antibody; MYL2 antibody; Myosin light chain 2 regulatory cardiac slow antibody; Myosin light polypeptide 2 regulatory cardiac slow antibody; Myosin regulatory light chain 2 antibody; Myosin regulatory light chain 2 ventricular/cardiac muscle isoform antibody; Regulatory light chain of myosin antibody; RLC of myosin antibody; Slow cardiac myosin regulatory light chain 2 antibody; ventricular/cardiac muscle isoform antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Myosin regulatory light chain 2, ventricular/cardiac muscle isoform protein (8-164AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
Biotin
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA
Protocols
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

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.
Gene References into Functions
  1. The hypocontractile activity of D94A MYL-2 mutant resulted in the rightward shift of the force-pCa dependence and decreased actin-activated myosin ATPase activity. PMID: 29463717
  2. 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
  3. 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
  4. 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
  5. 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
  6. 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
  7. Mutation in myosin regulatory light chain gene is associated with defective myosin motor function that ultimately result in pathological hypertrophic remodeling. PMID: 28467684
  8. 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
  9. 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
  10. Two siblings with hypertrophic cardiomyopathy had the pathogenic variant p.Ala13Thr variant in MYL2. PMID: 28223422
  11. 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
  12. FLNb enhances invasion of cancer cells through phosphorylation of MRLC and FAK. PMID: 25925610
  13. 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
  14. Myosin regulatory light chain phosphorylation enhances cardiac beta-myosin in vitro motility under load. PMID: 26116789
  15. 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
  16. 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
  17. 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
  18. 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
  19. an interplay between phosphorylation and glycosylation of MLC2, which might be involved in the development of muscle atrophy and associated changes PMID: 24184274
  20. 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
  21. 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
  22. NDRG1 inhibited an important regulatory pathway mediated by ROCK1/pMLC2 pathway that modulates stress fiber assembly. PMID: 23188716
  23. AMPK mediates spindle pole-associated pMRLC(ser19) to control spindle orientation via regulation of actin cortex-astral microtubule attachments PMID: 22688514
  24. MLC2 isoforms localisation is dependent on cell cycle in HeLa cells. PMID: 22425609
  25. 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
  26. 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
  27. This is the first report of mutations in TPM1, MY L3, and MYL2 associated with primary, non-hypertrophied restrictive cardiomyopathy. PMID: 21823217
  28. 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
  29. 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
  30. Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 have functional implications in platelets PMID: 20670370
  31. mutations in familial hypertrophic cardiomyopathy: phenotypic presentation and frequency in Danish and South African populations PMID: 11748309
  32. diphosphorylated MRLC and Rho-kinase accumulated and colocalized at the contractile ring and the midbody in dividing cells PMID: 12185584
  33. 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
  34. DLC1 negatively regulates Rho/ROCK/MLC2 PMID: 18648664
  35. Following down-regulation of MR-1, the phosphorylations of MLC2, focal adhesion kinase (FAK), and Akt were dramatically decreased PMID: 18948272
  36. 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
  37. 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
  38. 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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Involvement in disease
Cardiomyopathy, familial hypertrophic 10 (CMH10)
Subcellular Location
Cytoplasm, myofibril, sarcomere, A band.
Database Links

HGNC: 7583

OMIM: 160781

KEGG: hsa:4633

STRING: 9606.ENSP00000228841

UniGene: Hs.75535

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