Recombinant Human Myoglobin, Heme free, T7-tagged

• Cat.No.: MB-165H
• Product Overview: Recombinant Human Myo heme free produced inE.Coliis a non-glycosylated polypeptide chain. The protein has a molecular mass of 11.67kDa. The rHuMyo heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques.

Specification

• Cat. No.: MB-165H
• Description: Myoglobin 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. In 1958, John Kendrew and associates successfully determined the structure of myoglobin by high-resolution X-ray crystallography.
• Source: Escherichia Coli.
• Physical Appearance: Sterile Filtered solution.
• Formulation: The sterile solution (3.32mg/ml) contains phosphate-buffered saline (pH 8.0) and 50Mm phosphate-borate.
• Purity: Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Anion-exchange FPLC. (c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained.
• Dimers And Aggregates: Less than 1% as determined by silver stained SDS-PAGE gel analysis.
• Endotoxin: Less than 0.1 ng/µg (IEU/µg) of rHuMyo.
• Stability: rMyo heme free although stable at 15℃ for 2 weeks, should be stored at 4℃. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please do not freeze.

Gene Information

• Gene Name: MB myoglobin [ Homo sapiens ]
• Synonyms: MB; myoglobin; PVALB; MGC13548; OTTHUMP00000197922
• Gene ID: 4151
• mRNA Refseq: NM_005368
• Protein Refseq: NP_005359
• MIM: 160000
• UniProt ID: P02144
• Chromosome Location: 22q13.1
• Function: heme binding; metal ion binding; oxygen binding; oxygen transporter activity

Reviews

08/05/2020

Effective in pull-down assay.

07/01/2020

Perfect for my experiments.

07/26/2018

High-quality product, very satisfied.

Q&As

How does the structure of myoglobin facilitate its function in muscle tissues?

Myoglobin's structure, with a single heme group, allows it to bind oxygen tightly, facilitating its role in oxygen storage and release in muscle tissues.

Why is myoglobin considered a marker for muscle injury, especially in the context of myocardial infarction?

Myoglobin is released into the bloodstream when muscle cells are damaged. In the context of a myocardial infarction (heart attack), damaged heart muscle cells release myoglobin, making it a quick, albeit non-specific, marker for muscle injury.

How is myoglobin's affinity for oxygen influenced by environmental conditions?

Myoglobin's affinity for oxygen remains relatively constant across various environmental conditions, ensuring a steady oxygen supply for muscles even under stress.

Are there any known diseases or conditions associated with mutations or dysregulation of MB?

While mutations in the MB gene are rare, they can lead to myoglobinuria, a condition where myoglobin is present in the urine, often after intense muscle activity.

What are the clinical implications of elevated myoglobin levels in blood tests?

Elevated myoglobin levels in blood tests can indicate muscle injury, including myocardial infarction. However, since myoglobin is also found in skeletal muscles, it is often used in conjunction with other markers to diagnose heart attacks.

How does myoglobin differ from hemoglobin in terms of oxygen binding and release?

While both myoglobin and hemoglobin bind oxygen, myoglobin has a higher affinity for oxygen and does not exhibit cooperative binding. This allows myoglobin to release oxygen under conditions where hemoglobin cannot, such as during intense muscle activity.

What is the primary function of the MB gene and its encoded protein?

The MB gene encodes the protein myoglobin, which is responsible for storing and releasing oxygen in muscle cells, especially in conditions of high oxygen demand.