M7773
Monoclonal Anti-Myoglobin antibody produced in mouse
clone MG-1, ascites fluid
Sinônimo(s):
Anti-PVALB
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About This Item
Produtos recomendados
fonte biológica
mouse
Nível de qualidade
conjugado
unconjugated
forma do anticorpo
ascites fluid
tipo de produto de anticorpo
primary antibodies
clone
MG-1, monoclonal
contém
15 mM sodium azide
reatividade de espécies
human
técnica(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using human skeletal muscle tissue
indirect ELISA: 1:10,000
Isotipo
IgG1
nº de adesão UniProt
Condições de expedição
dry ice
temperatura de armazenamento
−20°C
modificação pós-traducional do alvo
unmodified
Informações sobre genes
human ... MB(4151)
Descrição geral
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.
Imunogênio
Purified human skeletal muscle myoglobin.
Aplicação
Monoclonal Anti-Myoglobin antibody is suitable for use in western blot and protein arrays.
Ações bioquímicas/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.
Exoneração de responsabilidade
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 classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
nwg
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Certificados de análise (COA)
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Myoglobin
Redei GP
Encyclopedia of Genetics, Genomics, Proteomics, and Informatics, 1314-1314 (2008)
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
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
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
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
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