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Key Documents

Safety Information

M5696

Sigma-Aldrich

Myoglobin from equine skeletal muscle

BioUltra, 95-100% (SDS-PAGE)

Synonym(s):

Myoglobin from horse skeletal muscle

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25 MG
¥913.03
100 MG
¥3,043.46
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¥9,949.75

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25 MG
¥913.03
100 MG
¥3,043.46
500 MG
¥9,949.75

About This Item

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

¥913.03


Please contact Customer Service for Availability

Request a Bulk Order

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.

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1 of 4

This Item
SAE0063P5521A2237
assay

≥95% (HPLC)

assay

-

assay

-

assay

-

specific activity

≥7000 units/mg protein (At 37 °C with pNPP and DEA as the substrates)

specific activity

-

specific activity

≥2,000 DEA units/mg protein

specific activity

-

concentration

20 mg/mL (ready-to-use)

concentration

-

concentration

≥1.0 mg/mL

concentration

≥900 DEA units/mL

form

buffered aqueous solution (ready-to-use, 20 mg/ml)

form

solution (high-activity)

form

aqueous solution

form

buffered aqueous glycerol solution

shipped in

wet ice

shipped in

wet ice

shipped in

-

shipped in

dry ice

optimum pH

8.0(Stability), 9.8(Activity)

optimum pH

-

optimum pH

-

optimum pH

-

Application

Myoglobin from equine skeletal muscle has been used to induce acute kidney injury (AKI) in mice.[1] It has also been used as a standard for top down mass spectrometry.[2]
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. [3]

Biochem/physiol Actions

Myoglobin from horse skeletal muscle is a single chain heme protein containing 153 amino acid residues.[4][5] 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.[6]
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 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

Regulatory Information

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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
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
Protein Bioinformatics (2017)
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
Rhabdomyolysis induced AKI via the regulation of endoplasmic reticulum stress and oxidative stress in PTECs
Feng Y, et al.
Royal Society of Chemistry Advances, 6(111), 109639-109648 (2016)

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