Myoglobin Native Protein | MB native protein
Human Myoglobin
Gene Names
MB; PVALB; myoglobgin
Purity
Greater than 96.0%.
Synonyms
Myoglobin; Human Myoglobin; Myoglobin Human; MB; PVALB; MGC13548; MB native protein
Host
Human Cardiac Tissues
Purity/Purification
Greater than 96.0%.
Form/Format
The protein solution is in 0.05M phosphate buffer containing 0.15M NaCl and 0.09% NaN3 pH 7.5. Filtered through a 0.2 uM membrane.
Sterile Filtered red solution.
Sterile Filtered red solution.
Concentration
7.35 mg/ml (varies by lot)
Sequence Length
154
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.
Preparation and Storage
Human Myoglobin should be stored at 2-8 degree C.
Related Product Information for MB native protein
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.
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.
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.
Product Categories/Family for MB native protein
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
Molecular Weight
17,184 Da
NCBI Official Full Name
myoglobin
NCBI Official Synonym Full Names
myoglobin
NCBI Official Symbol
MB
NCBI Official Synonym Symbols
PVALB; myoglobgin
NCBI Protein Information
myoglobin
UniProt Protein Name
Myoglobin
Protein Family
UniProt Gene Name
MB
UniProt Entry Name
MYG_HUMAN
NCBI Description
This gene encodes a member of the globin superfamily and is expressed in skeletal and cardiac muscles. The encoded protein is a haemoprotein contributing to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. At least three alternatively spliced transcript variants encoding the same protein have been reported. [provided by RefSeq, Jul 2008]
Uniprot Description
MB: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Belongs to the globin family.
Protein type: Carrier
Chromosomal Location of Human Ortholog: 22q13.1
Molecular Function: iron ion binding; heme binding; oxygen binding; oxygen transporter activity
Biological Process: slow-twitch skeletal muscle fiber contraction; response to hydrogen peroxide; oxygen transport; heart development; response to hypoxia; brown fat cell differentiation; response to hormone stimulus; enucleate erythrocyte differentiation
Research Articles on MB
1. Data show that chimeric neuroglobin and myoglobin were generated by swapping a regulatory segment.
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Product Notes
The MB mb (Catalog #AAA143116) is a Native Protein produced from Human Cardiac Tissues and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Myoglobin, Native Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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