| Description | Human serum albumin (HSA) is a monomeric, globular, and α-helical protein that constitutes a major part of human blood plasma proteins. This single-chain polypeptide protein contains 585 amino acid residues and 17 internal disulfide bridges and one free cysteine.Human serum albumin undergoes Human serum albumin (HSA) is a monomeric, globular, and α-helical protein that constitutes a major part of human blood plasma proteins. This single-chain polypeptide protein contains 585 amino acid residues and 17 internal disulfide bridges and one free cysteine.Human serum albumin undergoes three different post-translational modifications: oxidation, glycation, and S-nitrosylation. Modifications usually occur on the surface of the globular protein, and do not significantly affect conformation. However, modification strongly affects binding of fatty acids and drug molecules.Application:Albumin solution human has been used as a supplement in RPMI 1640 media during polymorphonuclear cell (PMN) incubation. It has also been used as a culture media for the differentiation and maturation of monocyte-derived dendritic cells... Read More | Inquire | Inquire | Proteasome-activating peptide 1 TFA is a peptide and a potent proteasome activator. Proteasome-activating peptide 1 TFA increases the chymotrypsin-like proteasomal catalytic activity and, consequently, proteolytic rates both in vitro and in culture. Proteasome-activating peptide 1 TFA prevents Proteasome-activating peptide 1 TFA is a peptide and a potent proteasome activator. Proteasome-activating peptide 1 TFA increases the chymotrypsin-like proteasomal catalytic activity and, consequently, proteolytic rates both in vitro and in culture. Proteasome-activating peptide 1 TFA prevents protein aggregation in a cellular model of amyotrophic lateral sclerosis... Read More | BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L,BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Unlike egg-white avidin, which has a net positive charge at neutral pH and contains about 7% carbohydrate, streptavidin has almost no net charge at neutral pH, does not contain carbohydrate, and exhibits lower non-specific background. Streptavidin conjugates are widely used together with a conjugate of biotin for specific detection of a variety of proteins, protein motifs, nucleic acids and other molecules. This FITC-streptavidin conjugate was prepared by highly purified Streptavidin and free FITC was removed. Streptavidin (FITC) is a useful second-step reagent for the indirect immunofluorescent staining of cells in combination with biotinylated primary antibodies for flow cytometric analysis. Excitation at 488nm light leads to a fluorescence emission maximum of 520 nm.Recommended Usage：Every lot of Streptavidin-FITC is tested by flow cytometry using biotinylated primary antibodies. From this testing it is recommended that between 0.02 and 0.25 µg of streptavidin be used per 106 cells in a 100 µl staining volume... Read More |