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| Catalog # | Availability | Size | Quantity | Unit Price | Save For Later Wish List | |
|---|---|---|---|---|---|---|
| RCP1439-20 | 7 days | 20 µg | $120.00 |
Select product before adding to cart
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| RCP1439-100 | 7 days | 100 µg | $290.00 | |||
| RCP1439-1 | 7 days | 1 mg | $1,584.00 |
Product Overview | |
| Name | Myo Human w/o H |
|---|---|
| Description | |
| Myoglobin (Heme free) Human Recombinant | |
| Accession (Primary) | P02144 |
| Synonyms | |
| Myoglobin, MB, PVALB, MGC13548. | |
| Introduction | |
| Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin’s molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure. | |
| Source | |
| Human Cardiac Tissues. | |
| Physical Appearance | |
| Sterile Filtered red solution. | |
| Formulation | |
| The protein solution is in 0.05M phosphate buffer pH 7.5 containing 0.15M NaCl and 0.09% NaN3. Filtered through a 0.2 µM membrane. | |
| Stability | |
| Human Myoglobin should be stored at 2-8°C. | |
| Purity | |
| Greater than 96.0%. | |
| Human Virus Test | |
| Starting material donor tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies. | |
| Precautions | |
| Myo Human w/o H is for research use only and not for use in diagnostic or therapeutic procedures. | |
Target Information: ( P02144 ) | |
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Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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ADMEbio Team
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ADMEbio Team
