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Merck

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

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

Product Name

Myoglobin from equine skeletal muscle, 95-100%, essentially salt-free, lyophilized powder

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.

P68082

storage temp.

−20°C

Quality Level

300

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

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
0000508486
0000508486
0000495242
0000495242
0000493897

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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
Y H Guan et al.
Journal of chromatography. A, 1217(21), 3525-3530 (2010-04-20)
Separation of large bioactive molecules such as proteins, DNAs and RNAs using aqueous two-phase systems (ATPSs) and liquid-liquid partition-based counter-current chromatography (CCC) can avoid risks of sample loss and denaturation, and greatly reduce processing time. We have constructed toroidal columns
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
The absorption spectra and extinction coefficients of myoglobin.
W J BOWEN
The Journal of biological chemistry, 179(1), 235-245 (1949-05-01)
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