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M0630

Sigma-Aldrich

Myoglobin from equine skeletal muscle

95-100%, essentially salt-free, lyophilized powder

Sinónimos:

Myoglobin from horse skeletal muscle

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About This Item

Número de CAS:
100684-32-0
Número CE:
309-705-0
Número MDL:
MFCD00131643
Código UNSPSC:
12352202
NACRES:
NA.61

origen biológico

equine skeletal muscle

Análisis

95-100%

formulario

essentially salt-free, lyophilized powder

mol peso

~17 kDa(lit.)

contenido de hierro

0.25-0.32%

técnicas

mass spectrometry (MS): suitable

solubilidad

H2O: soluble 10 mg/mL

Nº de acceso UniProt

P68082

temp. de almacenamiento

−20°C

Información sobre el gen

horse ... MB(100054434)

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Aplicación

Myoglobin from equine skeletal muscle was used in a study to test experimental protein mixture for validating tandem mass spectral analysis.

Acciones bioquímicas o fisiológicas

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.

Aplicación

Referencia del producto
Descripción
Precios

796-0657

Proteins, mixture, application for HPLC

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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
Ru Fang et al.
Journal of nanobiotechnology, 9, 19-19 (2011-05-19)
The synthesis of bioactive nanoparticles with precise molecular level control is a major challenge in bionanotechnology. Understanding the nature of the interactions between the active components and transport biomaterials is thus essential for the rational formulation of bio-nanocarriers. The current
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
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
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Chromatograms

application for HPLC

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