| Product Name | Human Myosin-10 (MYH10) ELISA Kit |
|---|---|
| Description | Myh10 was abundantly expressed in mouse brain and testis. It was also expressed in heart, lung, liver, and kidney, but not in skeletal muscle or spleen.Actin-activated MgATPase activity was decreased in MYH10 with either an asn97-to-lysine substitution, which is homologous to the N93K mutation in MYH9 that causes May-Hegglin anomaly , or an arg709-to-cysteine substitution, which causes developmental defects in brain and heart when present in mouse Myh10. The ability of MYH10 heavy meromyosin to support the movement of actin filaments over an MYH10-coated surface was reduced in heavy meromyosin with the N97K mutation and eliminated with the R709C mutation. Kinetic analysis indicated that the R709C mutation resulted in extremely tight affinity between MYH10 heavy meromyosin and ADP, reducing the rate of ADP release. This assay has high sensitivity and excellent specificity for detection of Human MYH10. No significant cross-reactivity or interference between Human MYH10 and analogues was observed. |
| Synonyms | MGC134913, MGC134914, NMMHCB, cellular myosin heavy chain, type B type B|myosin heavy chain, nonmuscle type B|myosin, heavy polypeptide 10, non-muscle|near to the ATP binding region|nonmuscle myosin |
| Method | Sandwich ELISA |
| Detection Range | 0.156-10 ng/mL |
| Sensitivity | 0.055 ng/mL |
| Reactivity | Human |
| Sample Types | Serum, Plasma, Other biological fluids. |
| Background | Myh10 was abundantly expressed in mouse brain and testis. It was also expressed in heart, lung, liver, and kidney, but not in skeletal muscle or spleen.Actin-activated MgATPase activity was decreased in MYH10 with either an asn97-to-lysine substitution, which is homologous to the N93K mutation in MYH9 that causes May-Hegglin anomaly , or an arg709-to-cysteine substitution, which causes developmental defects in brain and heart when present in mouse Myh10. The ability of MYH10 heavy meromyosin to support the movement of actin filaments over an MYH10-coated surface was reduced in heavy meromyosin with the N97K mutation and eliminated with the R709C mutation. Kinetic analysis indicated that the R709C mutation resulted in extremely tight affinity between MYH10 heavy meromyosin and ADP, reducing the rate of ADP release. |
| Supplier | Abebio |
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