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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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250 MG
HUF 34,200.00
1 G
HUF 115,000.00
5 G
HUF 379,000.00
10 G
HUF 622,000.00

HUF 34,200.00


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250 MG
HUF 34,200.00
1 G
HUF 115,000.00
5 G
HUF 379,000.00
10 G
HUF 622,000.00

About This Item

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

HUF 34,200.00


Please contact Customer Service for Availability

Request a Bulk Order

biological source

equine skeletal muscle

Quality Level

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)

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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.[1]

Biochem/physiol Actions

Myoglobin from horse skeletal muscle is a single chain heme protein containing 153 amino acid residues.[2] 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.[3]
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

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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
R A Masaracchia et al.
The Journal of parasitology, 72(2), 299-305 (1986-04-01)
Calmodulin was purified from the obliquely striated skeletal muscle of Ascaris suum. The calmodulin had a molecular weight of 16,400 and the amino acid composition indicated it is highly similar to other purified calmodulins, showing insignificant variation in 12 of
The absorption spectra and extinction coefficients of myoglobin.
W J BOWEN
The Journal of biological chemistry, 179(1), 235-245 (1949-05-01)

Articles

Professors summarize recent 2D materials synthesis advancements and biosensing applications in various fields.

Chromatograms

application for HPLC

Questions

1–3 of 3 Questions  
  1. Can you advise what the % level of hemoglobin (if any will be present in this product)? Or can this be treated as Hb contaminant free.

    1 answer
    1. While this product is not specifically tested for hemoglobin, it is purified by Sephadex gel filtration. Given the molecular weight differences between these two compounds, the presence of hemoglobin is highly unlikely.

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  2. Can you share the amino acid sequence of this protein? M0630

    1 answer
    1. This product is a native protein that has not been modified during the extraction and purification process. The sequence of this product is published information. Please refer to the information in the UniProt database: https://www.uniprot.org/uniprotkb/P68082/entry

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  3. Is this myoglobin detectable using immunoenzymatic assay?

    1 answer
    1. Unfortunately, none of the equine myoglobin products have been tested for suitability in ELISA. Performance of these products in immunoenzymatic assays cannot be validated.

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