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Merck
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Key Documents

M5696

Sigma-Aldrich

Myoglobin from equine skeletal muscle

BioUltra, 95-100% (SDS-PAGE)

Sinónimos:

Myoglobin from horse skeletal muscle

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About This Item

Número de CAS:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

equine skeletal muscle

product line

BioUltra

assay

95-100% (SDS-PAGE)

form

essentially salt-free, lyophilized powder

mol wt

~17 kDa(lit.)

purified by

affinity chromatography

Iron content content

~0.30%

technique(s)

mass spectrometry (MS): suitable

solubility

H2O: soluble 10 mg/mL

UniProt accession no.

storage temp.

−20°C

Gene Information

horse ... MB(100054434)

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Application

Myoglobin from equine skeletal muscle has been used to induce acute kidney injury (AKI) in mice. It has also been used as a standard for top down mass spectrometry.
Myoglobin is used as a molecular weight marker and a standard for mass spectroscopy and X-ray crystallography.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.
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_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Protein Bioinformatics (2017)
Seok Jong Song et al.
International journal of molecular sciences, 21(22) (2020-11-19)
A recent study showed that early renal tubular injury is ameliorated in Nod-like receptor pyrin domain-containing protein 3 (NLRP3) KO mice with rhabdomyolysis-induced acute kidney injury (RIAKI). However, the precise mechanism has not been determined. Therefore, we investigated the role
S C Powell et al.
Journal of chromatography, 317, 87-92 (1984-12-28)
Urine and serum myoglobin have been separated on an anion-exchange column, packed by the slurry technique. Urine or serum was injected directly into the column and eluted isocratically with Tris buffer. Freshly prepared myoglobin from human muscle gives two peaks
J Zaia et al.
Rapid communications in mass spectrometry : RCM, 6(1), 32-36 (1992-01-01)
Myoglobins from horse heart muscle, horse skeletal muscle and sperm whale are widely used as calibration standards or test compounds for various mass spectrometric methodologies. In all such cases reported in the literature, a molecular weight value is used (16,950.5
Z K Shihabi
Journal of chromatography. B, Biomedical applications, 669(1), 53-58 (1995-07-07)
Capillary electrophoresis was used in this study to separate urinary myoglobin from hemoglobin based on its electrophoretic mobility. Urine was applied directly without any treatment. The separation was accomplished in less than 7 min. Myoglobin extracted from human muscle tissues

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Chromatograms

application for HPLC

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