myoglobin Antibody (6): sc-101520
- myoglobin Antibody (6) is a mouse monoclonal IgG1 κ provided at 200 µg/ml
- raised against recombinant myoglobin of human origin
- recommended for detection of myoglobin of human origin by WB, IP and ELISA
- m-IgG Fc BP-HRP is the preferred secondary detection reagent for myoglobin Antibody (6) for WB applications. This reagent is now offered in a bundle with myoglobin Antibody (6) (see ordering information below).
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Myoglobin Antibody (6) is a mouse monoclonal IgG1 antibody that detects myoglobin in human samples through applications such as western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-myoglobin antibody (6) recognizes a crucial cytosolic oxygen-binding protein primarily found in skeletal and cardiac muscle, where myoglobin plays a vital role in the storage and diffusion of oxygen within myocytes. Myoglobin (6) monoclonal antibody enables research into a protein essential for maintaining mitochondrial respiration during intense and prolonged contractile activity, effectively transporting oxygen from erythrocytes to mitochondria, which is critical for energy production in muscle cells. The structure of myoglobin, characterized by its globular shape and heme group, allows oxygen binding efficiently, and evolutionary conservation across various species underscores myoglobin′s fundamental importance in muscle physiology. Anti-myoglobin antibody (6) provides reliable detection and quantification of myoglobin, facilitating research into muscle function and related pathologies.
Alexa Fluor® is a trademark of Molecular Probes Inc., OR., USA
LI-COR® and Odyssey® are registered trademarks of LI-COR Biosciences
myoglobin Antibody (6) References:
- The structural dynamics of myoglobin. | Brunori, M., et al. 2004. J Struct Biol. 147: 223-34. PMID: 15450292
- Hypoxia reprograms calcium signaling and regulates myoglobin expression. | Kanatous, SB., et al. 2009. Am J Physiol Cell Physiol. 296: C393-402. PMID: 19005161
- Role of heme in the unfolding and assembly of myoglobin. | Culbertson, DS. and Olson, JS. 2010. Biochemistry. 49: 6052-63. PMID: 20540498
- Synthesis of iron nanoparticles from hemoglobin and myoglobin. | Sayyad, AS., et al. 2012. Nanotechnology. 23: 055602. PMID: 22236554
- Palmitate interaction with physiological states of myoglobin. | Shih, L., et al. 2014. Biochim Biophys Acta. 1840: 656-66. PMID: 24482816
- Metastable photoproducts from carbon monoxide myoglobin. | Rousseau, DL. and Argade, PV. 1986. Proc Natl Acad Sci U S A. 83: 1310-4. PMID: 3456590
- Fatty acid binding of myoglobin depends on its oxygenation. | Götz, FM., et al. 1994. Biol Chem Hoppe Seyler. 375: 387-92. PMID: 7980870
- Quantitation of myoglobin saturation in the perfused heart using myoglobin as an optical inner filter. | Leisey, JR., et al. 1994. Am J Physiol. 267: H645-53. PMID: 8067420
- Myoglobin content of hamster skeletal muscles. | Meng, H., et al. 1993. J Appl Physiol (1985). 74: 2194-7. PMID: 8393001
- Myoglobin in pelagic small cetaceans. | Dolar, ML., et al. 1999. J Exp Biol. 202: 227-36. PMID: 9882635
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
myoglobin Antibody (6) | sc-101520 | 200 µg/ml | $322.00 | |||
myoglobin Antibody (6): m-IgG Fc BP-HRP Bundle | sc-539776 | 200 µg Ab; 10 µg BP | $361.00 |