M1882
Myoglobin from equine heart
≥90% (SDS-PAGE), essentially salt-free, lyophilized powder
Sinónimos:
Myoglobin from horse heart
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Acerca de este artículo
Form:
essentially salt-free, lyophilized powder
Assay:
≥90% (SDS-PAGE)
Biological source:
equine heart
Servicio técnico
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Permítanos ayudarlebiological source
equine heart
Quality Level
assay
≥90% (SDS-PAGE)
form
essentially salt-free, lyophilized powder
Iron content
≥0.20%
technique(s)
MALDI-MS: suitable
UniProt accession no.
storage temp.
−20°C
Gene Information
horse ... MB(100054434)
Application
Myoglobin from equine heart is suitable for use in:
- spectral measurements in Beckman DU-50 or Gilford 2400 spectrophotometer
- the secondary structure analysis of proteins in H2O solution using single-pass attenuated total reflection Fourier transform infrared (ATR-FT-IR) microscopy
- the calibration of the mass scale at a concentration of 2 pmol/μL in Electrospray mass spectrometry
- a study to investigate on-line single droplet deposition for MALDI mass spectrometry
- a study to examine protein adsorption in fused-silica and polyacrylamide-coated capillaries
Biochem/physiol Actions
Myoglobin is a mobile carrier of oxygen that is developed in red muscle and heart cells. This happens as a response to elevated demand for oxygen during exercise, and transports oxygen from the sarcolemma to the mitochondria of vertebrate heart and red muscle cells.
Clase de almacenamiento
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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D H Robertson et al.
Rapid communications in mass spectrometry : RCM, 11(7), 786-790 (1997-01-01)
Major urinary proteins (MUPs) from the urine of individual wild mice were characterized using electrospray ionization mass spectrometry (ESI-MS) and compared to MUPs from the urine of inbred mice. The wild mice showed considerable variation between individuals in the expression
Laurent Marichal et al.
Langmuir : the ACS journal of surfaces and colloids, 36(28), 8218-8230 (2020-06-26)
Protein adsorption on nanoparticles is an important field of study, particularly with regard to nanomedicine and nanotoxicology. Many factors can influence the composition and structure of the layer(s) of adsorbed proteins, the so-called protein corona. However, the role of protein
Ursula Waack et al.
mBio, 9(6) (2018-12-20)
Antibiotic-resistant Acinetobacter baumannii is increasingly recognized as a cause of difficult-to-treat nosocomial infections, including pneumonia, wound infections, and bacteremia. Previous studies have demonstrated that the metalloprotease CpaA contributes to virulence and prolongs clotting time when added to human plasma as