人肌红蛋白|Human Myoglobin

人肌红蛋白|Human Myoglobin
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 (ironcontaining
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.
Description
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.
Source Human Cardiac Tissues.
Physical
Appearance Sterile Filtered red solution.
Formulation 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.
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. Product tested and found
negative for HTLV antibodies.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY.
The product may not be used as drugs, agricultural or pesticidal products, food
additives or household chemicals.
Related
Products
» Myo Human w/o H
» Myoglobin Human