MYOGLOBIN

Product Name: Myoglobin
Synonyms: Myoglobin horse ; Myoglobin equine heart ; Myoglobin ; Myoglobin equine ; Apomyoglobin ; Myoglobin from sheep skeletal muscle ; Apomyoglobin, mass spec standard ; Apomyoglobin from horse skeletal muscle
Product Categories: Standards for Protein Sequencing;Protein Sequencing;Protein Structural Analysis
Molecular Weight:
CAS NO: 9008-45-1
Molecular Weight:17 000
EINECS: 232-935-7
Mol File: Mol File
Storage temp. −20°C
Solubility : H₂O: 10 mg/mL, clear, red to red-brown
Form :  Myoglobin (CAS NO. 9008-45-1) is essentially salt-free, lyophilized powder.

In 1958, John Kendrew and associates successfully determined the structure of myoglobin by high-resolution X-ray crystallography.For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz. Despite being one of the most studied proteins in biology, its true physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin are viable, but showed a 30% reduction in cardiac systolic output. They adapted to this deficiency through hypoxic genetic mechanisms and increased vasodilation.

Hazard Codes B
Safety Statements 22-24/25
S22:Do not breathe dust. 
S24/25:Avoid contact with skin and eyes.  
WGK Germany 3
F 3-8-10-23

Myoglobin (CAS NO. 9008-45-1) is a protein that in humans is encoded by the MB gene.
Myoglobin (CAS NO. 9008-45-1) is a single-chain globular protein of 153 amino acids, containing a heme (iron-containing porphyrin) prosthetic group in the center around which the remaining apoprotein folds. It has eight alpha helices and a hydrophobic core. It has a molecular weight of 16,700 daltons, and is the primary oxygen-carrying pigment of muscle tissues. Unlike the blood-borne hemoglobin, to which it is structurally related,this protein does not exhibit cooperative binding of oxygen, since positive cooperativity is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is unaffected by the oxygen pressure in the surrounding tissue. Myoglobin is often cited as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. High concentrations of myoglobin in muscle cells allow organisms to hold their breaths longer.