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Native Human Myoglobin

Cat.No.: MB-4460H
Product Overview: Human Myoglobin produced in Human Cardiac Tissues having a molecular mass of 17.5kDa. Myoglobin is released from recently injured myocardial cells within a few hours of Infarction. Peak levels are reached more quickly than CK-MB or Troponin complex.
Description: 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. Myoglobinμs 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.
Source: Human Cardiac Tissues.
Species: Human
Form: The protein solution is in 0.05M phosphate buffer containing 0.15M NaCl and 0.09% NaN3 pH 7.5. Filtered through a 0.2μM membrane.
Molecular Mass: 17.5kDa
Purity: Greater than 96.0%.
Stability: Human Myoglobin should be stored at 2-8°C.
Gene Name: MB myoglobin [ Homo sapiens ]
Official Symbol: MB
Synonyms: MB; myoglobin; PVALB; MGC13548;
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;

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