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SYPRO® Ruby Protein Gel Stain

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Synonym(s):
SYPRO® dye, protein gel stain
UNSPSC Code:
41105322
NACRES:
NA.32

shelf life

≥6 mo. (when stored at room temperature and protected from light)

Quality Level

technique(s)

protein staining: suitable

fluorescence

λex 280,450 nm; λem 610 nm

General description

SYPRO Ruby protein gel stain is a ready-to-use, ultrasensitive, luminescent stain for the detection of proteins separated by polyacrylamide gel electrophoresis (PAGE). This stain, designed especially for use in 2-D PAGE, has proven to be an excellent choice for 1-D PAGE and isoelectric focusing (IEF) gels as well. SYPRO Ruby protein gel stain attains sensitivity comparable to many silver stain techniques. However, unlike silver staining, the SYPRO Ruby gel stain:
  • uses a simple staining protocol, with no possibility of overstaining
  • delivers a linear quantitation range of over three orders of magnitude
  • shows less protein-to-protein variability
  • stains glycoproteins, lipoproteins, calcium-binding proteins, fibrillar proteins, and other difficult-to-stain proteins
  • will not stain extraneous nucleic acids
  • does not interfere with subsequent analysis of proteins by Edman-based sequencing or mass spectrometry

Application

SYPRO ruby protein gel stain has been used for staining of the proteins after sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE).

Caution

Protect from light.

Legal Information

SYPRO is a registered trademark of Life Technologies

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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Filipe Natalio et al.
Cell and tissue research, 339(2), 429-436 (2009-12-17)
Primmorphs (a three-dimensional sponge primary cell culture system) have been revealed to be a cell/tissue nano-factory for the production of tailor-made hybrid nanostructures. Growth of primmorphs is stimulated by the presence of a titanium alkoxide precursor tolerating titania (TiO2) concentrations
Chronic hypoxia alters mitochondrial composition in human macrophages.
Fuhrmann DC, et al.
Biochimica et Biophysica Acta, 1834, 2750-2760 (2013)
Jun Zou et al.
eLife, 4, e09406-e09406 (2015-10-17)
Truncating mutations in the giant sarcomeric protein Titin result in dilated cardiomyopathy and skeletal myopathy. The most severely affected dilated cardiomyopathy patients harbor Titin truncations in the C-terminal two-thirds of the protein, suggesting that mutation position might influence disease mechanism.
Jennifer Osten et al.
The Journal of general physiology, 154(10) (2022-09-03)
The β-myosin heavy chain expressed in ventricular myocardium and the myosin heavy chain (MyHC) in slow-twitch skeletal Musculus soleus (M. soleus) type-I fibers are both encoded by MYH7. Thus, these myosin molecules are deemed equivalent. However, some reports suggested variations
Saskia Hutten et al.
Cell reports, 33(12), 108538-108538 (2020-12-29)
Nuclear import receptors, also called importins, mediate nuclear import of proteins and chaperone aggregation-prone cargoes (e.g., neurodegeneration-linked RNA-binding proteins [RBPs]) in the cytoplasm. Importins were identified as modulators of cellular toxicity elicited by arginine-rich dipeptide repeat proteins (DPRs), an aberrant

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