Heavy Meromyosin (HMM)
(Actin Binding Protein fragment)
| Protein | Heavy Meromyosin (fragment of Myosin II from m. psoas) |
| Origin | Skeletal muscle, rabbit |
| Molecular mass | 150 kDa |
| Protein description |
Heavy Meromyosin (HMM) is produced by limited chymotryptic cleavage of myosin II isolated from rabbit psoas muscle. The resulting motor fragment has an apparent molecular mass of approximately 150 kDa and comprises the two myosin head domains, which contain the actin- and ATP-binding sites, together with the proximal S2 region. Each heavy chain is associated with one essential light chain (ELC) and one regulatory light chain (RLC). HMM retains the ATP-dependent actin-binding and motor activity of myosin II and is widely used in actomyosin research. In electron microscopy, decoration of actin filaments with HMM provides a reliable method to determine filament polarity, as the characteristic arrowhead pattern reveals the orientation of the actin filament. |
| Actin interaction | Binds specifically to F-actin through the myosin head domains; binding is ATP-dependent and supports HMM decoration of actin filaments for polarity determination. |
| Form | Lyophilized, ready-to-use. |
| Quantity per unit | 2x 100 µg |
| Buffer | 50 mM KCl, 10 mM Tris pH 7.6, 0.2 mM DTT and 1% disaccharides, when 100 µg is reconstituted with 100 µl ultrapure water. |
| Purity | >96% by scanning densitometry from Coomassie G-250 stained SDS-Gels. |
| Purification notes | Purified from rabbit skeletal muscle (m. psoas). |
| Protein concentration | Determined by UV absorbance: 1 mg/ml corresponds to A278 = 0.6 ml/mg |
| Storage instructions | Upon reconstitution the product is stored on ice. This product can also be stored as a glycerol stock at −20 °C. Avoid repeated freeze / thaw cycles. |
| Shipping conditions | At ambient temperature. Upon delivery store at −70 °C. |
| Remarks | For Use in Research only. Not for Use in Human or Veterinary Diagnostical or Therapeutical Applications. |
| CAS no. | |
Proteins and buffers from Hypermol® are made of the ultrapure reagents in Milli-Q™ water, as described in our publications.
