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Validated All-in-One™ qPCR Primer for MYH9(NM_002473.5) Search again
Product ID:
HQP011614
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
BDPLT6, DFNA17, EPSTS, FTNS, MATINS, MHA, NMHC-II-A, NMMHC-IIA, NMMHCA
Gene Description:
myosin heavy chain 9
Target Gene Accession:
NM_002473.5(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain. The protein is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in MYH9 are the cause of non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness.
Gene References into function
- mutations cause a spectrum of autosomal dominant macrothrombocytopenias: May-Hegglin anomaly and Fechtner, Sebastian, Epstein, and Alport-like syndromes; hence, the name "MYHIIA syndrome" is proposed to encompass all of these disorders
- mutation in epstein syndrome
- Motor protein nonmuscle myosin heavy chain-IIA and CXCR$ colocalize at the leading edge of migrating T lymphocytes, together with filamentous actin and myosin light chain.
- A major role is indicated for the NMMHC-IIA abnormality in the pathogenesis of leukocyte, platelet, and kidney defects in Fechtner syndrome.
- A single base pair transition in MYH9, resulting in an amino acid substitution D1424N, is responsible for macrothrombocytopenia and hearing loss in the kindred under study.
- The Asp1424Asn mutation in the MYH9 gene causes the May-Hegglin anomaly, Fechtner syndrome, Sebastian syndrome, & Epstein syndrome, which result from a highly unstable protein & failure to reorganize the megakaryocyte cytoskeleton for platelet production
- MYH9 gene is implicated in May-Hegglin anomaly, Sebastian syndrome, Fechtner syndrome and Epstein syndrome which are autosomal dominant macrothrombocytopenias.
- In a case of anaplastic large cell lymphoma, a portion of MYH9 is found to be fused to the ALK gene in a novel chromosomal abnormality, t(2;22)(p23;q11.2).
- Myosin heavy polypeptide 9 (MYH9) colocalizes with actin stress fibers in mammalian cells.
- sCD163-NMMHCA complexes were present in activated T lymphocytes after incubation with shed sCD163
- Here targeted gene disruption was performed to understand fundamental as well as pathological role of the gene for NMMHCA, MYH9.
- Two cleavage sites on NMHC-A, Asp-1153 and Asp-1948, at which it is cleaved during apoptosis, were determined.
- Casein kinase 2 phosphorylation of the myosin-IIA heavy chain protects against Ca2+-regulated S100 family member MTS1-induced filament disassembly and inhibition of assembly of nonmuscle myosin-IIA filaments.
- Haploinsufficiency of NMMHC-IIA in megakaryocytic lineage is the mechanism of macrothrombocytopenia consequent to MYH9 mutations, whereas in granulocytes a dominant-negative effect of mutant allele is involved in the formation of inclusion bodies.
- VEGF, extracellular matrix, and intracellular motor protein MyH9 are all essential for the novel function of nucleolin in angiogenesis.
- Results suggest that MYH9 mediates the binding of oviductal glycoprotein to human sperm.
- Mutation of MYH9 gene exists in cases of Chinese MYH9-related disease. In the two families, the point mutation was located in exon 38(G5521A), and the transference rule of the MYH9 gene mutation is corresponding with clinical phenotype distribution.
- myosin IIA and IIB isoforms are regulated by different signaling pathways to perform distinct cellular activities
- Patients carrying R702 mutations had significantly larger platelets than those with other MYH9 mutations
- Myosin IIA negatively regulates cell migration and maintains a balance between the actomyosin and microtubule systems by regulating microtubule dynamics.
- MIIA plays a role in CXCR4 endocytosis, which involves its dynamic association with beta-arrestin and highlights the role of endogenous MIIA as a regulator of CXCR4 internalization and, therefore, the onset of SDF-1alpha signaling.
- Pairwise and multilocus haplotype analyses identified linkage disequilibrium between polymorphism alleles at the MYH9 locus and the disease.
- direct platelet myosin IIA participation in internal contraction
- These observations support a direct role for myosin-IIA heavy-chain phosphorylation in mediating motility and chemotaxis.
- MyosinIIa contractility is required for maintenance of platelet structure during spreading on collagen and contributes to thrombus stability
- myosin IIA is required for a critical step between NK immunological synapse formation and granule exocytosis
- An MYH9 human disease model in flies.
- subjects with mutations in the motor domain present with severe thrombocytopenia and develop nephritis and deafness before the age of 40, while those with mutations in the tail domain have a much lower risk of complications and higher platelet counts
- show the differential expression of mutant NMMHC-IIA and postulate that cell-specific regulation mechanisms function in MYH9 disorders
- during T lymphocyte migration, uropodal adhesion depends on LFA-1 avidity, where MyH9 serves as a key mechanical link between LFA-1 and the cytoskeleton that is critical for LFA-1 de-adhesion
- first report of a large deletion of the MYH9 gene leading to the development of MYH9 disorders
- The effects of MYH9-siRNA-induced suppression underline the critical role of NMHC-IIA in maintenance of cell shape and adhesion.
- On both RBCs and microbeads, human CD47 potently inhibits phagocytosis as does direct inhibition of myosin. CD47-SIRPalpha interaction initiates a dephosphorylation cascade directed in part at phosphotyrosine in myosin.
- TRPM7 regulates myosin IIA filament stability and localization by phosphorylating a short stretch of amino acids within the alpha-helical tail of the myosin IIA heavy chain
- Expression of full-length human NMHC-IIA and -IIB in 10 T1/2 cells demonstrated that flectin antibody recognizes both isoforms
- The highest LOD score was found in chromosomal region 22q12.2-12.3 and the total linkage area spans over 20 cM; this region contains the MYH9 gene, which is expressed in the developing palate.
- proplatelet formation in human megakaryocytes undergoes a complex spatio-temporal regulation orchestrated by adhesive proteins, GPIb-IX-V and myosin IIA
- Genetic variation at the MYH9 locus is associated with nondiabetic end-stage kidney diseases.
- Genetic variation at the MYH9 locus substantially explains the increased burden of focal segmental glomerulosclerosis and hypertensive end-stage kidney diseases.
- patients developed CLL clones with identical antibody V regions, suggesting selection by a common antigen. Monoclonal antibodies from this stereotypics subset are reactive MYHIIA
- Data show that swapping a small C-terminal portion of the tail between myosin IIA and IIB inverts the distinct distribution of these isoforms in migrating cells.
- results demonstrate that both the 6S/10S conformational change and the tailpiece contribute to the localization and assembly of myosin II in mammalian cells
- These observations indicate multiple functions for NM IIA which involve previously unrecognized control of intracellular signaling and protein expression.