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The BLUEstain™ Protein ladder is a three-color protein standard with 12 prestained proteins covering a wide range molecular weights from ~11 to 245 kDa. Proteins are covalently coupled with a bluechromophore except for two reference bands (one green and one red band at 25 kDa and 75 kDa respectively) when separated on SDS-PAGE (Tris-glycine buffer). The BLUEstain™ Protein ladder, is designed for monitoring protein separation during SDS-polyacrylamide gel electrophoresis, verification of Western transfer efficiency on membranes (PVDF, nylon, or nitrocellulose) and for approximating the size of proteins. The ladder is supplied in gel loading buffer and is ready to use.

Agarose LE (Low Electroendosmosis) is Molecular Biology Grade and is specifically designed for the superior separation of nucleic acids, with maximally crisp band resolution, and is also ideal for cloning and cloning related experiments.

GoldBio Agarose LE is refined in an advanced process that excludes the use of organic solvents. The result is a cleaner end-product with significantly reduced environmental impact. The agarose can be used for analyses of nucleic acids from 50 bp to 25 kbp, protein electrophoresis and various blotting protocols.

The low EEO of the agarose promotes increased electrophoretic mobility, yielding improved resolution and shorter run times. This also allows macromolecules and larger particles (subcellular fragments, viruses, etc.) to migrate more freely through the gel matrix. The consistently low EEO reduces band distortion (caused by counterflow) that can result from the presence of excessive sulfate-rich negative ions.

Agarose is a natural product that forms an inert matrix used in electrophoresis, chromatography and other molecular biology and biochemistry techniques. Likewise, it is neutral and easily derivatizable, so it is easy to bind to its structure proteins like enzymes, antigens or antibodies. Toxicity absence makes working with agarose very convenient.

Dithiothreitol (DTT) is the common name of the more popular of the two Cleland’s Reagents (the other being Dithioerythritol or DTE). DTT is a powerful reducing agent that forms a stable six-membered ring with an internal disulfide bond which is resistant to oxidation. DTT is often used for the following: reducing the disulfide bridge of the cross-linker N,N′-bis(acryloyl) cystamine to break apart the matrix of a polyacrylamide gel, the reduction of disulfide bonds in proteins, the prevention of those bonds from forming between cysteine residues and lastly, DTT is often used to reduce thiolated DNA in order to minimize dimerization.

DTT is a nearly 7-fold stronger reduction agent than βME (β-mercaptoethanol) and has a less offensive odor and is less toxic.

Kanamycin is an aminoglycoside antibiotic isolated from Streptomyces kanamyceticus. It is effective against gram-positive and gram-negative bacteria as well as Mycoplasma species. Kanamycin is commonly used to select for bacteria that have been transformed with a kanamycin-resistant gene and plant tissues that have the NPT II (APH3) gene incorporated in them. Kanamycin is very soluble in aqueous solution and is typically used in concentrations of 50-100 µg/ml.

Proteinase K is a highly reactive nonspecific serine protease that belongs to the subtilisin family of proteins. It cleaves at the carboxylic acid side of aliphatic, aromatic, or hydrophobic amino acids. Proteinase K is capable of inactivating RNases and DNases and is used in the isolation or preparation of high molecular weight nucleic acids. Proteinase K is also useful for helping to characterize enzymes, due to its cleavage specificity. This enzyme was designated proteinase K because of its ability to hydrolyze keratin. Proteinase K is stable in a wide variety of detergents and buffer salts and at various temperatures and pH. The isoelectric point of proteinase K is 8.9.

TCEP-HCl is an odorless reducing agent suitable for protein applications and in the preparation for electrophoresis. TCEP is water soluble, is stable in a variety of solutions and is particularly useful in the labeling of cysteine residues with maleimides, preventing the cysteines from forming disulfide bonds. As a reducing agent, TCEP has many other desirable features.