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M0630

Sigma-Aldrich

Myoglobin from equine skeletal muscle

95-100%, essentially salt-free, lyophilized powder

Synonym(s):

Myoglobin from horse skeletal muscle

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About This Item

CAS Number:
100684-32-0
EC Number:
309-705-0
MDL number:
MFCD00131643
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

equine skeletal muscle

Quality Level

300

Assay

95-100%

form

essentially salt-free, lyophilized powder

mol wt

~17 kDa(lit.)

Iron content

0.25-0.32%

technique(s)

mass spectrometry (MS): suitable

solubility

H2O: soluble 10 mg/mL

UniProt accession no.

P68082

storage temp.

−20°C

Gene Information

horse ... MB(100054434)

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Application

Myoglobin from equine skeletal muscle was used in a study to test experimental protein mixture for validating tandem mass spectral analysis.

Biochem/physiol Actions

Myoglobin from horse skeletal muscle is a single chain heme protein containing 153 amino acid residues. It possesses no disulfide bridges or free -SH groups. Myoglobin contains 8 variously sized right-handed helical regions, joined by non-ordered or random coil regions.
Myoglobin is critical to skeletal muscle O2 supply at near-maximum oxygen demand, and prevents anoxia by maintaining PO2 above levels needed to support mitochondrial function.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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L Henry et al.
Structural dynamics (Melville, N.Y.), 7(5), 054702-054702 (2020-09-29)
The correct folding of proteins is of paramount importance for their function, and protein misfolding is believed to be the primary cause of a wide range of diseases. Protein folding has been investigated with time-averaged methods and time-resolved spectroscopy, but
Emily S Choy et al.
The Journal of experimental biology, 222(Pt 11) (2019-05-18)
Arctic marine ecosystems are currently undergoing rapid environmental changes. Over the past 20 years, individual growth rates of beluga whales (Delphinapterus leucas) have declined, which may be a response to climate change; however, the scarcity of physiological data makes it difficult
Anthony W Maresso et al.
PLoS pathogens, 4(8), e1000132-e1000132 (2008-08-30)
Acquisition of iron is necessary for the replication of nearly all bacterial pathogens; however, iron of vertebrate hosts is mostly sequestered by heme and bound to hemoglobin within red blood cells. In Bacillus anthracis, the spore-forming agent of anthrax, the
The absorption spectra and extinction coefficients of myoglobin.
W J BOWEN
The Journal of biological chemistry, 179(1), 235-245 (1949-05-01)
Ru Fang et al.
Journal of nanobiotechnology, 9, 19-19 (2011-05-19)
The synthesis of bioactive nanoparticles with precise molecular level control is a major challenge in bionanotechnology. Understanding the nature of the interactions between the active components and transport biomaterials is thus essential for the rational formulation of bio-nanocarriers. The current
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Chromatograms

application for HPLC

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