50 ?g

N-Lauroylsarcosine Sodium Salt

N-Lauroylsarcosine

N-Lauroylsarcosine is an anionic detergent.

N-Lauroylsarcosine, Sodium Salt

N-Propyl Gallate

Cross-linking agent for preparation of polyacrylamide gels for electrophoresis

Naproxen

Niclosamide

NZ Bovine Fibrinogen, 90% Clottable

O-Phenylenediamine

Oleic Acid, cell culture reagent

Orcinol Monohydrate

Oxytetracycline hydrochloride

P-Dimethylamino-Benzaldehyde

P-Nitrophenyl Phosphate, Disodium Salt Hexahydrate

p-Phenylenediamine

Pepsin

PHENYL ISOTHIOCYANATE

Pluronic® F-68

Ponceau 2R

Ponceau S, dye content: ~75%

Primaquine diphosphate

Probucol

Procaine Hydrochloride

Pyridoxine Hydrochloride

Quinine Hemisulfate

Quinine Hydrochloride

RESAZURIN

Rotenone

Rubidium Chloride

SANTONIN

Sephadex® G-10

Sephadex® G-100

Sephadex G-25

Sodium Borohydride

Sodium Borohydride

Sodium Diatrizoate

Sodium Dodecyl Sulfate

SODIUM METHACRYLATE

SODIUM SELENATE

Solvent Blue 35

Streptomycin Sulfate

Sulfanilic acid

Sulfasalazine

Sulforhodamine B, cell culture reagent

SULFUR, 99.999%

Thermo Scientific Pierce Coomassie Brilliant Blue dyes are composed of one of the most common forms of coomassie dye, which is a key component of various colorimetric protein gel stains. Coomassie R-250 and G-250 dyes are two chemical forms of a disulfonated triphenylmethane compound that is commonly used as the basis of stains for detection of proteins in gel electrophoresis and Bradford-type assay reagents for protein quantitation. The R-250 (red-tinted) form lacks two methyl groups that are present in the G-250 (green-tinted) form, which is also called colloidal coomassie dye.

Coomassie R-250 and G-250 dyes are two chemical forms of a disulfonated triphenylmethane compound that is commonly used as the basis of stains for detection of proteins in gel electrophoresis and Bradford-type assay reagents for protein quantitation. The R-250 (red-tinted) form lacks two methyl groups that are present in the G-250 (green-tinted) form, which is also called colloidal coomassie dye.

Typically, coomassie gel stains and protein assay reagents are formulated as very acidic solutions in 25 to 50% methanol. In acidic conditions, the dye binds to proteins primarily through basic amino acids (primarily arginine, lysine, and histidine), and the number of coomassie dye ligands bound to each protein molecule is approximately proportional to the number of positive charges found on the protein. Protein binding causes the dye to change from reddish-brown to bright blue (absorption maximum equals 595 nm).

Features include:
• Easy detection—develops intensely colored complexes with proteins
• High sensitivity—can determine as little as 0.5 μg/cm2 of protein present in a gel matrix
• Reversible staining—anion of Coomassie Brilliant Blue dye formed in the acidic staining medium combines with the protonated amino groups of proteins by electrostatic interaction; resulting complex is reversible under proper conditions
• Differentiation between bound and unbound dye—when dissolved in 0.01 M citrate buffer at pH 3.0, has an absorption maximum at 555 nm; protein-dye complex is characterized by a peak slightly broader than that of free dye with a maximum at 549 nm

Trifluoromethanesulfonic acid

Tris

Tyloxapol