Myoglobin His Human
Description
MB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Myoglobin is a small, monomeric protein with a molecular weight of approximately 17.8 kDa. It consists of a single polypeptide chain of 154 amino acids and contains a heme prosthetic group, which is responsible for its oxygen-binding properties. The heme group consists of an iron ion (Fe2+) coordinated within a porphyrin ring. This iron ion is capable of binding to one oxygen molecule (O2), allowing myoglobin to store and transport oxygen within muscle cells.
The structure of myoglobin is highly conserved across different species, reflecting its essential role in muscle physiology. The protein’s tertiary structure is composed of eight alpha-helices, which create a hydrophobic pocket for the heme group. This pocket protects the heme iron from oxidation and ensures efficient oxygen binding and release.
Recombinant human myoglobin His is a form of myoglobin that has been genetically engineered to include a histidine (His) tag at the N-terminus. This His-tag is a short sequence of histidine residues that facilitates the purification of the protein using affinity chromatography techniques. The recombinant protein is typically expressed in Escherichia coli (E. coli) and purified to high purity levels, often exceeding 90% as determined by SDS-PAGE analysis .
The amino acid sequence of recombinant human myoglobin His corresponds to the full-length human myoglobin protein, with the addition of the His-tag. The sequence is as follows:
MGSSHHHHHH SSGLVPRGSH MGLSDGEWQL VLNVWGKVEA DIPGHGQEVL IRLFKGHPET LEKFDKFKHL KSEDEMKASE DLKKHGATVL TALGGILKKK GHHEAEIKPL AQSHATKHKI PVKYLEFISE CIIQVLQSKH PGDFGADAQG AMNKALELFR KDMASNYKEL GFQG
Recombinant human myoglobin His is widely used in biochemical and biophysical research. Some of its key applications include:
- Structural Studies: The high purity and well-defined structure of recombinant myoglobin make it an ideal model for studying protein folding, stability, and dynamics.
- Oxygen Binding Studies: Researchers use recombinant myoglobin to investigate the mechanisms of oxygen binding and release, as well as the effects of mutations on these processes.
- Drug Development: Myoglobin can serve as a target for developing drugs that modulate oxygen delivery to tissues, which may have therapeutic potential in conditions such as ischemia and hypoxia.
- Biotechnology: The His-tagged version of myoglobin is used in various biotechnological applications, including the development of biosensors and the production of recombinant proteins.
Recombinant human myoglobin His is typically supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 1 mM DTT, 10% glycerol, and 100 mM NaCl. It is recommended to store the protein at 4°C for short-term use and at -20°C for long-term storage. To maintain its stability and activity, it is important to avoid repeated freeze-thaw cycles .
