Human Myoglobin ELISA Kit is a single-wash 90-min Simplestep used to quantify Human Myoglobin with a sensitivity of 270 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step.
- Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader
- Design your own immunoassay: we also offer the conjugation-ready antibody pair
- Cited in over 5 citations
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application sELISA | 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
Human Myoglobin ELISA Kit is a single-wash 90-min Simplestep used to quantify Human Myoglobin with a sensitivity of 270 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step.
- Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader
- Design your own immunoassay: we also offer the conjugation-ready antibody pair
- Cited in over 5 citations
Sample | n | mean | SD | C.V. |
---|---|---|---|---|
Sample Homogenate | n 5 | mean - | SD - | C.V. 2 |
Sample | n | mean | SD | C.V. |
---|---|---|---|---|
Sample Homogenate | n 3 | mean - | SD - | C.V. 2 |
Sample type | Average % | Range |
---|---|---|
Sample type Serum | Average % = 103 | Range 83 - 115 % |
Sample type Urine | Average % = 75 | Range 67 - 81 % |
Sample type Tissue Extracts | Average % = 111 | Range 105 - 118 % |
Sample type Cell culture media | Average % = 101 | Range 81 - 113 % |
Sample type Citrate plasma | Average % = 99 | Range 82 - 108 % |
Sample type EDTA Plasma | Average % = 98 | Range 90 - 110 % |
Sample type Heparin Plasma | Average % = 89 | Range 86 - 92 % |
Human Myoglobin ELISA kit (ab171580) is a single-wash 90 min sandwich ELISA designed for the quantitative measurement of Myoglobin protein in human serum, plasma, urine, cell culture supernatant, cell and tissue extracts. It uses our proprietary SimpleStep ELISA® technology. Quantitate human myoglobin with 270 pg/ml sensitivity.
SimpleStep ELISA® technology employs capture antibodies conjugated to an affinity tag that is recognized by the monoclonal antibody used to coat our SimpleStep ELISA® plates. This approach to sandwich ELISA allows the formation of the antibody-analyte sandwich complex in a single step, significantly reducing assay time. See the SimpleStep ELISA® protocol summary in the image section for further details. Our SimpleStep ELISA® technology provides several benefits:
-Single-wash protocol reduces assay time to 90 minutes or less
-High sensitivity, specificity and reproducibility from superior antibodies
-Fully validated in biological samples
-96-wells plate breakable into 12 x 8 wells strips
A 384-well SimpleStep ELISA® microplate (Pre-coated 384 well Microplate SimpleStep ELISA® ab203359) is available to use as an alternative to the 96-well microplate provided with SimpeStep ELISA® kits.
Myoglobin, a heme protein is found in both cardiac and skeletal muscle and functions as a reserve supply of oxygen by facilitating the movement of oxygen within muscles. Damage to either type of muscle following conditions such as trauma, ischemia, and diseases that cause myopathy, is associated with the release of myoglobin into serum. Specifically, following cardiac necrosis associated with myocardial infarction (MI), myoglobin is one of the first markers to rise above normal levels. Myoglobin levels increase measurably above baseline within 2-4 hours post-infarct, peaking at 9-12 hours, and returning to baseline within 24-36 hours.
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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Example of human Myoglobin standard curve in Sample Diluent NS.
The Myoglobin standard curve was prepared as described in Section 10. Raw data values are shown in the table. Background-subtracted data values (mean +/- SD) are graphed.
Interpolated concentrations of native Myoglobin in human serum and plasma samples.
The concentrations of Myoglobin were measured in duplicates, interpolated from the Myoglobin standard curves and corrected for sample dilution. Undiluted samples are as follows: serum 25%, plasma (heparin) 25%, plasma (citrate) 25%, plasma (EDTA) 25%. The interpolated dilution factor corrected values are plotted (mean +/- SD, n=2). The mean Myoglobin concentration was determined to be 15.8 ng/mL in serum, 15.6 ng/mL in plasma (citrate), 8.3 ng/mL in plasma (EDTA) and 3.4 ng/mL in plasma (heparin).
Serum from ten individual healthy human female donors was measured in duplicate.
Interpolated dilution factor corrected values are plotted (mean +/- SD, n=2). 5 of 10 donors were below the detectable dose. The mean Myoglobin concentration was determined to be 5.4 ng/mL with a range of ND – 9.8 ng/mL.
Interpolated concentrations of spike Myoglobin in human cell culture media and urine samples.
The concentrations of Myoglobin were measured in duplicates, interpolated from the Myoglobin standard curves and corrected for sample dilution. Undiluted samples are as follows: cell culture media 25% and urine 25%. The interpolated dilution factor corrected values are plotted (mean +/- SD, n=2).
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