M7773
Monoclonal Anti-Myoglobin antibody produced in mouse
clone MG-1, ascites fluid
Sinónimos:
Anti-PVALB
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About This Item
Productos recomendados
origen biológico
mouse
Nivel de calidad
conjugado
unconjugated
forma del anticuerpo
ascites fluid
tipo de anticuerpo
primary antibodies
clon
MG-1, monoclonal
contiene
15 mM sodium azide
reactividad de especies
human
técnicas
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using human skeletal muscle tissue
indirect ELISA: 1:10,000
isotipo
IgG1
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−20°C
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... MB(4151)
Descripción general
Myoglobin is a hemoprotein that regulates the storage and diffusion of oxygen in heart and skeletal muscles. Additionally, this protein also protects the tissues from oxidative damage by controlling the levels of reactive oxygen species and nitric oxide. Thus, myoglobin has been implicated in regulating nitric oxide and oxygen levels in the mitochondrial compartments of skeletal muscle and cardiac cells. Monoclonal Anti-Myoglobin antibody is specific for myoglobin and stains human skeletal muscles. The product does not cross-react with hemoglobin.
Myoglobin is composed of a 153 amino acid long polypeptide and heme group. This protein is encoded by the gene MB mapped to human chromosome 22q12.3. It is a unit of 20S core proteasome complex. Myoglobin is localized to the skeletal and cardiac muscle.
Inmunógeno
Purified human skeletal muscle myoglobin.
Aplicación
Monoclonal Anti-Myoglobin antibody is suitable for use in western blot and protein arrays.
Acciones bioquímicas o fisiológicas
Myoglobin participates in proteases mediated degradation of intracellular proteins Upon damage to the muscle cell due to infarction of a coronary artery, neurological trauma, infection or tumor processes, myoglobin escapes to the environment and can be found in plasma using sensitive assays.
Cláusula de descargo de responsabilidad
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
nwg
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
U B Hendgen-Cotta et al.
The Journal of experimental biology, 213(Pt 16), 2734-2740 (2010-08-03)
For more than 100 years, myoglobin has been among the most extensively studied proteins. Since the first comprehensive review on myoglobin function as a dioxygen store by Millikan in 1939 and the discovery of its structure 50 years ago, multiple
Myoglobin
Redei GP
Encyclopedia of Genetics, Genomics, Proteomics, and Informatics, 1314-1314 (2008)
George A Ordway et al.
The Journal of experimental biology, 207(Pt 20), 3441-3446 (2004-09-02)
Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging
Joy G Ghosh et al.
Protein science : a publication of the Protein Society, 14(3), 684-695 (2005-02-22)
Protein pin array technology was used to identify subunit-subunit interaction sites in the small heat shock protein (sHSP) alphaB crystallin. Subunit-subunit interaction sites were defined as consensus sequences that interacted with both human alphaA crystallin and alphaB crystallin. The human
D J Marcinek et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 280(4), R1123-R1133 (2001-03-15)
Myoglobin (Mb) buffers intracellular O2 and facilitates diffusion of O2 through the cell. These functions of Mb will be most effective when intracellular PO2 is near the partial pressure of oxygen at which Mb is half saturated (P50) of the
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