Chemicals & Small Molecules

Amphotericin B solution is a broad-spectrum polyene antifungal antibiotic which is unstable at room temperature and susceptible to degradation by light, heat, and acid. The solution exerts its strongest antifungal activity at pH 6.0 to 7.5. Amphotericin B binds to ergosterol on the fungal cell membrane, which will damage membrane, increase permeability, leak intracellular substances and disrupt normal metabolism. As bacterial cell membranes do not contain ergosterol, amphotericin B is ineffective against bacteria. TargetMol's amphotericin B solution is a sterile, filtered and ready-to-use solution for cell culture, containing 250 μg/mL of amphotericin B. It is recommended for use in cell culture application at 0.25-2.5 μg/mL of amphotericin B. Dilute the solution as experimental needs.

The production and breakdown of intracellular proteins is in dynamic equilibrium under stable environmental conditions and when proteins are extracted from cells and tissues in vitro, crude cell extracts contain many endogenous enzymes that are capable of degrading the target proteins, e.g. phosphatases and proteases. These enzymes are released from the cells or activated, leading to the breakdown of the target protein and affecting the results of the analysis. To avoid this, one way to increase the yield of target proteins is to incorporate inhibitors of the relevant enzymes. TargetMol Mass Spectrometry-Compatible Protease Inhibitor Cocktail has a solvent of ddH2O and consists of four components including Aprotinin, Bestatin, E-64 and Leupeptin, which have broad specificity for serine and cysteine proteases and aminopeptidases, and no EDTA. This product is free of AEBSF, which avoids the potential for peak drift in mass spectra. This product does not contain AEBSF, thus avoiding the p

The production and breakdown of intracellular proteins is in dynamic equilibrium under stable environmental conditions and when proteins are extracted from cells and tissues in vitro, crude cell extracts contain many endogenous enzymes that are capable of degrading the target proteins, e.g. phosphatases and proteases. These enzymes are released from the cells or are activated, leading to the breakdown of the target protein and affecting the results of the analysis. Therefore, adding appropriate inhibitors of proteases, phosphatases and other enzymes to the extracts is an effective way to prevent protein degradation and de-modification. TargetMol Protease Phosphatase Inhibitor Cocktail is a mixture of 5 protease inhibitors and 4 phosphatase inhibitors in ddH2O, which can efficiently inhibit a wide range of proteases including serine, cysteine proteases, and aminopeptidases, as well as a wide range of phosphatases including acid, alkaline, and serine/threonine phosphatases in protein ext

The production and breakdown of intracellular proteins is in dynamic equilibrium under stable environmental conditions and when proteins are extracted from cells and tissues in vitro, crude cell extracts contain many endogenous enzymes that are capable of degrading the target proteins, e.g. phosphatases and proteases. These enzymes are released from the cells or are activated, leading to the breakdown of the target protein and affecting the results of the analysis. Therefore, adding appropriate inhibitors of proteases, phosphatases and other enzymes to the extracts is an effective way to prevent protein degradation and de-modification. TargetMol Protease Phosphatase Inhibitor Cocktail, with ddH2O as solvent, is a mixture of 4 protease inhibitors and 4 phosphatase inhibitors, which can efficiently inhibit a variety of proteases including serine, cysteine proteases and aminopeptidases, as well as a variety of phosphatases including acidic, alkaline, and serine/threonine phosphatases in p

Targetmol's Flag Tag Agarose contain a mouse-derived anti-DYKDDDDK (Flag) monoclonal antibody densely and directionally coupled to the surface of highly crosslinked agarose gel microspheres, which specifically binds to Flag-tagged proteins. Targetmol's Flag Tag agarose can be used for immunoprecipitation (IP) and co-immunoprecipitation (Co-IP) of proteins and protein complexes, as well as for antibody purification. It is suitable for antigenic samples from cell lysates, cell secretion supernatants, serum, ascites and other sources.

Targetmol's Myc Tag Agarose contain a mouse-derived Myc monoclonal antibody densely and directionally coupled to the surface of highly crosslinked agarose gel microspheres, which specifically binds to Flag-tagged proteins. Targetmol's Myc Tag agarose can be used for immunoprecipitation (IP) and co-immunoprecipitation (Co-IP) of proteins and protein complexes, as well as for antibody purification. It is suitable for antigenic samples from cell lysates, cell secretion supernatants, serum, ascites and other sources.

Targetmol's HA Tag Agarose contain a mouse-derived HA monoclonal antibody densely and directionally coupled to the surface of highly crosslinked agarose gel microspheres, which specifically binds to Flag-tagged proteins. Targetmol's HA Tag agarose can be used for immunoprecipitation (IP) and co-immunoprecipitation (Co-IP) of proteins and protein complexes, as well as for antibody purification. It is suitable for antigenic samples from cell lysates, cell secretion supernatants, serum, ascites and other sources.

Targetmol's GST Tag Agarose use a highly cross-linked agarose gel as a matrix, chemically modified with a spacer arm of 12 atoms in length to covalently bind reduced glutathione. This design ensures high protein binding capacity and stability, and GST Tag Agarose Gels are specifically designed for the purification of GST Tag fusion recombinant proteins from different expression systems.

TargetMol's His Tag Agarose NTA-Nickel uses a highly crosslinked 4% agarose gel as a substrate to which nitrilotriacetic acid (NTA) is immobilised by chemical coupling. NTA chelates nickel ions (Ni²⁺) to form a stable planar quartet that provides multiple ligand sites for the imidazolium ring of histidine tags to efficiently bind target proteins. The His-tag Protein Purification Agarose Gel is suitable for the purification of histidine-tagged proteins, i.e. 6xHis-tag proteins, from a wide range of expression systems (e.g., E. coli, yeast, insect cells, and mammalian cells).