M0630
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
Form:
essentially salt-free, lyophilized powder
Assay:
95-100%
Biological source:
equine skeletal muscle
Mol wt:
~17 kDa(lit.)
Quality Level
biological source
equine skeletal muscle
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.
storage temp.
−20°C
Gene Information
horse ... MB(100054434)
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.
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Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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Related Content
Instructions
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
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
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| M0630-250MG | 04061833993477 |
| M0630-1G | 04061833993460 |
| M0630-5G | 04061833993484 |
| M0630-10G | 04061833993453 |