Recombinant Human Myoglobin Protein

Beta LifeScience SKU/CAT #: BL-3550PS
Recombinant Human Myoglobin Protein

Recombinant Human Myoglobin Protein

Beta LifeScience SKU/CAT #: BL-3550PS
Catalog No.: BL-3550PS

Product Overview

Tag N/A
Host Species Human
Synonym Myoglobin, MB, PVALB, MGC13548.
Background 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 153aa, 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.
Description Myoglobin Human Recombinant expressed in E.Coli is a non-glycosylated polypeptide chain having a molecular weight of 17.67 kDa. The Myoglobin is purified by unique purification methods.
Source E.coli
Purity >95.0% as determined bySDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Formulation The sterile solution contains phosphate-buffered saline (pH 7.4) and 0.05% NaN3.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage Myoglobin should be stored at 4°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please do not freeze.
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