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Key Documents

M7773

Sigma-Aldrich

Monoclonal Anti-Myoglobin antibody produced in mouse

clone MG-1, ascites fluid

Synonyme(s) :

Anti-PVALB

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Clone

MG-1, monoclonal

Contient

15 mM sodium azide

Espèces réactives

human

Technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using human skeletal muscle tissue
indirect ELISA: 1:10,000

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MB(4151)

Description générale

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.

Immunogène

Purified human skeletal muscle myoglobin.

Application

Monoclonal Anti-Myoglobin antibody is suitable for use in western blot and protein arrays.

Actions biochimiques/physiologiques

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.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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)
Proteomics analysis indicated the protein expression pattern related to the development of fetal conotruncal defects
Wu Y, et al.
Journal of Cellular Physiology, 234(8), 13544-13556 (2019)
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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