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SYPRO® Orange Protein Gel Stain

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Synonym(s):
SYPRO® dye, protein gel stain
EC Number:
200-664-3

shelf life

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

Quality Level

200

technique(s)

protein staining: suitable

fluorescence

λex 300,470 nm; λem 570 nm

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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).

Application

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.

Caution

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.
Description
Pricing

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

188.6 °F - closed cup

Flash Point(C)

87 °C - closed cup

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Xiahezi Kuai et al.
Frontiers in plant science, 8, 1715-1715 (2017-10-20)
Each year, crop yield is lost to weeds competing for resources, insect herbivory and diseases caused by pathogens. To thwart these insults and preserve yield security and a high quality of traits, conventional agriculture makes use of improved cultivars combined
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
Brijesh B Khadgi et al.
Nucleic acids research, 47(16), 8708-8719 (2019-08-09)
Long Interspersed Elements (LINEs), also known as non-LTR retrotransposons, encode a multifunctional protein that reverse transcribes its mRNA into DNA at the site of insertion by target primed reverse transcription. The second half of the integration reaction remains very poorly
Influence of GTP on system specific chaperone - Twin arginine signal peptide interaction.
Cherak SJ and Turner RJ
Biochemical and Biophysical Research Communications, 465, 753-757 (2015)
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
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