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M7773

Sigma-Aldrich

Monoclonal Anti-Myoglobin antibody produced in mouse

clone MG-1, ascites fluid

Synonym(s):

Anti-PVALB

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

MG-1, monoclonal

contains

15 mM sodium azide

species reactivity

human

technique(s)

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

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MB(4151)

General description

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.

Immunogen

Purified human skeletal muscle myoglobin.

Application

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

Biochem/physiol Actions

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.

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
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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