Description
Background
Myoglobin(MB) also known as PVALB, is a single-chain globular protein of 153 or 154 amino acids, containing a heme (iron-containing porphyrin)prosthetic group in the center around which the remaining apoprotein folds. Two structural variants of myoglobin were described by Boyer et al. (1963). Boulton et al. (1969) studied postmortem muscle from 2,500 persons. Twomyoglobin variants were found, and in one of these substitution of lysine for glutamic acid at residue 53 was demonstrated. Myoglobin was the first protein to have its three-dimensional structure revealed. Jeffreys et al. (1984) used DNA probes isolated from the cloned myoglobin gene to map the gene in human-rodent somatic cell hybrids. The myoglobinlocus mapped to chromosome 22q11-q13. Myoglobin is released from damaged muscle tissue (rhabdomyolysis), which has very high concentrations of myoglobin. The released myoglobin is filtered by the kidneys but is toxic to the renal tubular epithelium and so may cause acute renal failure.
Data Sheet
| Form | lyophilized |
| Ig type | rabbit IgG |
| Immunogen/Antigen | A synthetic peptide corresponding to a sequence at the C-terminal |
| Reconstitution | 0.2ml of distilled water will yield a concentration of 500μg/ml. |
| Size | 100ug/vial |
| Storage | At -20C for one year. After reconstitution, at 4C for one month. |
