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Merck

S4942

SYPRO Ruby Protein Gel Stain

Synonym(s):

protein gel stain, SYPRO dye

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About This Item

NACRES:
NA.32
UNSPSC Code:
41105322
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shelf life

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

technique(s)

protein staining: suitable

fluorescence

λex 280,450 nm; λem 610 nm

Quality Level

Application

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

Disclaimer

Protect from light.

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

Legal Information

SYPRO is a trademark of Thermo-Fisher Scientific, Inc.

Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Christoph Schröder et al.
Methods in molecular biology (Clifton, N.J.), 785, 203-221 (2011-09-09)
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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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