Recombinant Human Myoglobin Protein Standard (His tag) is a Human Fragment protein, expressed in Escherichia coli, with >=80% purity and suitable for sELISA, SDS-PAGE.
>=80% SDS-PAGE
Escherichia coli
His tag C-Terminus
sELISA, SDS-PAGE
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application sELISA | Reactivity Reacts | Dilution info - | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:30918256, PubMed:34679218). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (PubMed:32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:34679218).
Myoglobin, Nitrite reductase MB, Pseudoperoxidase MB, MB
Recombinant Human Myoglobin Protein Standard (His tag) is a Human Fragment protein, expressed in Escherichia coli, with >=80% purity and suitable for sELISA, SDS-PAGE.
>=80% SDS-PAGE
Escherichia coli
His tag C-Terminus
sELISA, SDS-PAGE
No
Yes
Human
pH: 7.3 - 7.5
Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic
Fragment
18.5 kDa
Recombinant
His tag C-Terminus
Liquid
Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:30918256, PubMed:34679218). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (PubMed:32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:34679218).
Belongs to the globin family.
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.
This supplementary information is collated from multiple sources and compiled automatically.
Myoglobin also known as MB is a small globular protein with a molecular weight of approximately 17 kDa. It functions as an oxygen-binding protein and is expressed mainly in cardiac and skeletal muscle tissue where it facilitates oxygen storage and transport. The myoglobin protein plays an important role in maintaining the oxygen supply needed during muscular contraction and intense physical activity.
Myoglobin in muscle cells acts to store oxygen which provides a rapid release when required during muscle contraction. Myoglobin serves as a monomer and does not form part of a complex. Its structure allows it to temporarily store and relay oxygen where it is most required enhancing the often abrupt demands of muscles for oxygen. The ability of myoglobin to bind oxygen and release it under hypoxic conditions is central to its biological role in vertebrates.
The function of myoglobin in aerobic respiration in muscles involves its participation in the oxygen transport pathway. This protein closely interacts with hemoglobin to mobilize oxygen effectively to mitochondria during muscle contraction. Unlike hemoglobin myoglobin has a hyperbolic oxygen dissociation curve which allows it to provide oxygen at lower partial pressures contributing significantly to the efficient metabolism during hypoxia or intense muscular exertion.
Myoglobin plays a significant role in conditions such as rhabdomyolysis and myocardial infarction. Rhabdomyolysis a syndrome caused by muscle injury results in the release of myoglobin into the bloodstream. Myoglobin detection kits including myoglobin ELISA are essential tools for the diagnosis of these conditions. Moreover its rapid increase in plasma levels after heart muscle damage enables its use as an early marker for myocardial infarction. Myoglobin's interaction with proteins like creatine kinase provides valuable information on muscle damage and cardiac events.
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SDS-PAGE analysis of ab316414
Sandwich ELISA with the capture antibody dilution at 2 ug/mL and detector antibody dilution at 0.5 ug/mL.
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