M7659
Myosin Heavy Chain from rabbit muscle
buffered aqueous glycerol solution
Synonym(s):
ATPase inactive whole chain myosin
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About This Item
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biological source
rabbit muscle
form
buffered aqueous glycerol solution
technique(s)
electrophoresis: suitable
UniProt accession no.
foreign activity
ATPase Activity ≤0.01 units/mg protein
storage temp.
−20°C
Gene Information
rabbit ... PBV1SPCR2(100009284)
General description
Myosin heavy chain (MHC) is a motor protein of muscle thick filaments. MHC regulates ultrastructural diversity of myofibrils.
Application
Myosin Heavy Chain from rabbit muscle has been used:
- in SDS analysis of myosin heavy chain (MHC) composition and content
- for microinjection into the outflow of heart (blood serum) and the cephalic cavities (embryonic cerebrospinal fluid) of chick embryo
- as a muscle protein, to study the role of ascorbate as a facilitator of glycogen storage in muscles
Biochem/physiol Actions
Molecular motor involved in the contraction of muscles.
Physical form
Solution in 50% glycerol containing 0.6 M KCl and 0.005 M potassium phosphate, pH 6.5
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Morphological and biochemical alterations of skeletal muscles from the genetically obese (ob/ob) mouse
Kemp JG, et al.
International journal of obesity (2005), 33(8), 831-831 (2009)
L Wells et al.
The EMBO journal, 15(17), 4454-4459 (1996-09-02)
Myosin heavy chain (MHC) is the motor protein of muscle thick filaments. Most organisms produce many muscle MHC isoforms with temporally and spatially regulated expression patterns. This suggests that isoforms of MHC have different characteristics necessary for defining specific muscle
A blood-CSF barrier function controls embryonic CSF protein composition and homeostasis during early CNS development
Parvas M, et al.
Developmental Biology, 321(1), 51-63 (2008)
Myosin heavy chain isoforms regulate muscle function but not myofibril assembly.
Wells L, et al.
The Embo Journal, 15(17), 4454-4459 (1996)
I Morano
Journal of molecular medicine (Berlin, Germany), 77(7), 544-555 (1999-09-24)
Cardiac contraction is triggered by the cyclic interaction of the "molecular motor" protein myosin with the actin filament, consuming ATP as the energy source to produce tension or shortening. The myosin heavy chain (MHC) contains the actin- and ATP-binding sites
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