|Product Overview :
||Recombinant Human Myoglobin produced in E. coli cells is a single non-glycosylated polypeptide chain containing 166 amino acids. rhMyoglobin has a molecular mass of 18.7 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques at GenScript.
||Myoglobin, a member of the globin family of proteins, is a cytosolic oxygen-binding protein that regulates the storage and diffusion of oxygen within myocytes. The largest expression of myoglobin is in skeletal and cardiac muscle. Myoglobin exhibits various functions in relation to the muscular oxygen supply, such as oxygen storage, facilitated diffusion, and myoglobin-mediated oxidative phosphorylation. Myoglobin is the primary oxygen-carrying pigment of muscle tissues. High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with a particularly high abundance of myoglobin. Myoglobin is found in Type I, Type II A and Type II B muscle; however several studies indicate myoglobinis not found in smooth muscle.
|Molecular Mass :
|AA Sequence :
MHHHHHHDDD DKMGLSDGEW QLVLNVWGKV EADIPGHGQE VLIRLFKGHP ETLEKFDKFK HLKSEDEMKA SEDLKKHGAT VLTALGGILK KKGHHEAEIK PLAQSHATKH KIPVKYLEFI SECIIQVLQS KHPGDFGADA QGAMNKALEL FRKDMASNYK ELGFQG
||< 0.2 EU/μg, determined by LAL method.
||> 95% as analyzed by SDS-PAGE
||Stable up to 6 months at lower than -70 centigrade from date of receipt.
Stable up to 1 week at 4 centigrade or up to 3 months at -20 centigrade.
|Storage Buffer :
||Liquid after a 0.22 μm filtered solution in 20 mM Tris-HCl, 1 mM DTT, 100 mM NaC land 20% glycerol, pH 8.0.