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SYPRO® Orange Protein Gel Stain

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SYPRO® dye, protein gel stain
EC Number:

shelf life

≥6 mo. (when stored desiccated and protected from light at room temperature, 4 °C or 20 °C.)

Quality Level


protein staining: suitable


λex 300,470 nm; λem 570 nm

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SYPRO® Orange Protein Gel Stain



SYPRO® Ruby Protein Gel Stain





λex 300,470 nm; λem 570 nm




λex 280,450 nm; λem 610 nm



shelf life

≥6 mo. (when stored desiccated and protected from light at room temperature, 4 °C or 20 °C.)

shelf life


shelf life

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

shelf life


General description

SYPRO Orange is similar to SYPRO Red although it is somewhat brighter and gives slightly higher background fluorescence. For those using a laser-excited gel scanner, an argon-ion laser-based instrument is recommended for SYPRO Orange. The dye is efficiently excited by UV or broad band illumination. It is not suitable for staining proteins on blots or in IEF gels and shows reduced sensitivity when staining proteins on 2-D gels.
SYPRO Orange is:
  • Highly sensitive. The stain can detect 1 to 2 ng of protein per minigel band, making it more sensitive than Coomassie Brilliant Blue or silver staining.
  • Rapid. Staining is complete in less than one hour
  • Simple. After electrophoresis, the gel is stained, rinsed and photographed; no fixation or destaining steps are required
  • Compatible with standard laboratory equipment. Stained proteins can be visualized with a standard 300 nm UV transilluminator or laser scanner.
  • Cost-effective. Staining with SYPRO Orange is less expensive than silver staining and requires less time.
  • Low protein-to-protein variability. The dye interacts with the SDS coat around the protein, giving more consistent staining between different types of proteins compared to Coomassie or silver staining.
  • Selective for proteins. SYPRO Orange detects proteins as small as 6.5 kDa and does not stain nucleic acids or lipopolysaccharides. It does stain glycosylated proteins.
  • Broad linear range of detection. The fluorescence intensity of the stained bands is linear with protein quantity over three orders of magnitude (a much broader range than either Coomassie or silver staining).


SYPRO orange protein gel stain has been used in the thermal denaturation assay and thermal shift assay of protein(s) of interest. It has also been used in differential scanning fluorimetry.


The SYPRO stock solutions should be stored desiccated and protected from light at room temperature, 4 °C or 20 °C. When stored properly, these stock solutions are stable for six months to one year. The staining reagent diluted in buffer or acetic acid solution can be stored in very clean and detergent-free glass or plastic bottles, protected from light at 4 °C for at least three months. 

Legal Information

SYPRO is a registered trademark of Life Technologies

related product

Product No.

Storage Class

10 - Combustible liquids




188.6 °F - closed cup


87 °C - closed cup

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Ruth Cohen-Khait et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(52), 14982-14987 (2016-12-14)
Protein-protein interactions occur via well-defined interfaces on the protein surface. Whereas the location of homologous interfaces is conserved, their composition varies, suggesting that multiple solutions may support high-affinity binding. In this study, we examined the plasticity of the interface of
Algal lectin binding to core (a1-6) fucosylated N-glycans: structural basis for specificity and production of recombinant protein.
do Nascimento AS, et al.
Glycobiology, 25, 607-616 (2015)
Glu121-Lys319 salt bridge between catalytic and N-terminal domains is pivotal for the activity and stability of Escherichia coli aminopeptidase N.
Gumpena R, et al.
Protein Science, 21, 727-736 (2012)
M Murshida Mahbub et al.
Mobile DNA, 8, 16-16 (2017-11-21)
R2 elements are a clade of early branching Long Interspersed Elements (LINEs). LINEs are retrotransposable elements whose replication can have profound effects on the genomes in which they reside. No crystal or EM structures exist for the reverse transcriptase (RT)
Mohammad M Rahman et al.
Journal of bacteriology, 201(20) (2019-07-31)
The gastric pathogen Helicobacter pylori has limited ability to use carbohydrates as a carbon source, relying instead on exogenous amino acids and peptides. Uptake of certain peptides by H. pylori requires an ATP binding cassette (ABC) transporter annotated dipeptide permease


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