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About This Item
Nom du produit
Apomyoglobin from equine skeletal muscle, Protein sequencing standard, lyophilized powder
form
lyophilized powder
mol wt
16,951 Da by calculation
packaging
vial of ~60 nmol
storage temp.
−20°C
Quality Level
Application
- Identification of carbonylation sites in apomyoglobin after exposure to 4-hydroxy-2-nonenal by solid-phase enrichment and liquid chromatography-electrospray ionization tandem mass spectrometry.: This research identifies specific carbonylation sites in apomyoglobin following exposure to 4-hydroxy-2-nonenal, using advanced mass spectrometry techniques for precise localization of oxidative modifications. (Rauniyar et al., 2010).
- Analysis of heterogeneous fluorescence decays in proteins. Using fluorescence lifetime of 8-anilino-1-naphthalenesulfonate to probe apomyoglobin unfolding at equilibrium.: This study uses fluorescence lifetime measurements to analyze the unfolding processes of apomyoglobin, providing insights into protein stability and folding dynamics. (Wang et al., 2006).
Preparation Note
Prepared by the method of Rothgeb and Gurd
Classe de stockage
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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Physical methods for the study of myoglobin.
T M Rothgeb et al.
Methods in enzymology, 52, 473-486 (1978-01-01)
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Thomas Kupke et al.
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Transmembrane signaling proteins play a crucial role in the transduction of information across cell membranes. One function of regulated intramembrane proteolysis (RIP) is the release of signaling factors from transmembrane proteins. To study the role of transmembrane domains (TMDs) in modulating
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