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S4942

Supelco

SYPRO® Ruby Protein Gel Stain

Synonym(s):

SYPRO® dye, protein gel stain

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About This Item

UNSPSC Code:
41105322
NACRES:
NA.32

shelf life

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

Quality Level

100

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

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Chronic hypoxia alters mitochondrial composition in human macrophages.
Fuhrmann DC, et al.
Biochimica et Biophysica Acta, 1834, 2750-2760 (2013)
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
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
Di Xiao et al.
iScience, 25(6), 104489-104489 (2022-06-21)
Myogenesis is governed by signaling networks that are tightly regulated in a time-dependent manner. Although different protein kinases have been identified, knowledge of the global signaling networks and their downstream substrates during myogenesis remains incomplete. Here, we map the myogenic
Michal Domanski et al.
Bio-protocol, 7(8) (2017-07-12)
The RNA exosome complex plays a central role in RNA processing and regulated turnover. Present both in cytoplasm and nucleus, the exosome functions through associations with ribonucleases and various adapter proteins (reviewed in [Kilchert et al., 2016]). The following protocol
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