Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. In humans, myoglobin is only found in the bloodstream after muscle injury. High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography. Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile, but show many cellular and physiological adaptations to overcome the loss. In humans, myoglobin is encoded by the MB gene. Myoglobin can take the forms oxymyoglobin (MbO2), carboxymyoglobin (MbCO), and metmyoglobin (met-Mb), analogously to hemoglobin taking the forms oxyhemoglobin (HbO2), carboxyhemoglobin (HbCO), and methemoglobin (met-Hb).
Background References
1. Servonnet A. et. al. Myoglobin: still a useful biomarker in 2017? Ann Biol Clin (Paris). 2018 Apr
2. Vargas DA. et. al. Myoglobin-Catalyzed C-H Functionalization of Unprotected Indoles. Angew Chem Int Ed Engl. 2018 Jul
Western blot analysis of Myoglobin on different lysates with Mouse anti-Myoglobin antibody (EM1902-27) at 1/1,000 dilution.
Lane 1: Mouse skeletal muscle tissue lysate Lane 2: Rat skeletal muscle tissue lysate Lane 3: Mouse heart tissue lysate Lane 4: Rat heart tissue lysate
Lysates/proteins at 40 µg/Lane.
Predicted band size: 17 kDa Observed band size: 17 kDa
Exposure time: 10 seconds; ECL: K1801;
4-20% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (EM1902-27) at 1/1,000 dilution was used in 5% NFDM/TBST at 4℃ overnight. Goat Anti-Mouse IgG - HRP Secondary Antibody (HA1006) at 1/50,000 dilution was used for 1 hour at room temperature.
Immunofluorescence staining of paraffin- embedded human fetal skeletal muscle tissue using anti-Myoglobin antibody.The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 10% negative goat serum for 1 hour at room temperature, washed with PBS, and then probed with EM1902-27 at 1/50 dilution for 10 hours at 4℃ and detected using Alexa Fluor® 488 conjugate-Goat anti-Mouse IgG (H+L) Secondary Antibody at a dilution of 1:500 for 1 hour at room temperature.
Immunohistochemical analysis of paraffin-embedded rat heart tissue using anti-Myoglobin antibody. The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 8.0-8.4) for 20 minutes.The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (EM1902-27, 1/100) for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
Immunohistochemical analysis of paraffin-embedded human fetal skeletal muscle tissue using anti-Myoglobin antibody. The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 8.0-8.4) for 20 minutes.The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (EM1902-27, 1/400) for 30 minutes at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
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