Proteins & Peptides

AACX2 is an Acetylated BSA which is part of the Signal Seeker line. Lysine residues of bovine serum albumin (BSA) have been chemically acetylated by acetic anhydride under basic conditions. A major Ac BSA band runs at approximately 66 KDa and Ac BSA oligos run at approximately 120 260 KDa. Acetylated BSA is supplied as a lyophilized powder.

AB07, Rabbit skeletal muscle actin (Cat. # AKL99) that has been modified to contain covalently linked biotin at random surface lysine residues. An activated ester of biotin is used to label the protein. The labeling stoichiometry has been determined to be approximately 1 biotin per actin monomer and has an approximate molecular weight of 43 kDa. AB07 is supplied as a lyophilized powder and when stored desiccated to < 10% humidity at 4°C is stable for 6 months. Uses for AB07 include: Microinjection into muscle cell followed by electron microscopy of streptavidin conjugated gold particles to determine the cellular localization of the modified actin. Microinjection into muscle cell followed by electron microscopy of streptavidin conjugated gold particles to determine the cellular localization of the modified actin. In vitro motility experiments using biotinylated seeds of F-actin bound to fluorescent beads for laser tweezer manipulation. Produce affinity columns using biotinylated F-actin

AB07, Rabbit skeletal muscle actin (Cat. # AKL99) that has been modified to contain covalently linked biotin at random surface lysine residues. An activated ester of biotin is used to label the protein. The labeling stoichiometry has been determined to be approximately 1 biotin per actin monomer and has an approximate molecular weight of 43 kDa. AB07 is supplied as a lyophilized powder and when stored desiccated to < 10% humidity at 4°C is stable for 6 months. Uses for AB07 include: Microinjection into muscle cell followed by electron microscopy of streptavidin conjugated gold particles to determine the cellular localization of the modified actin. Microinjection into muscle cell followed by electron microscopy of streptavidin conjugated gold particles to determine the cellular localization of the modified actin. In vitro motility experiments using biotinylated seeds of F-actin bound to fluorescent beads for laser tweezer manipulation. Produce affinity columns using biotinylated F-actin

Actins are highly conserved within the eukaryotic kingdom and exist in higher eukaryotes as multigene families. The different actin isoforms can show distinct cellular and sub-cellular expression and localization. It has been demonstrated that different isoforms have subtly different biochemical properties in vitro which supports functional diversity within isotypes in vivo. Monomeric actin (G-actin) can self assemble (polymerize) into microfilaments (F-actin), the fundamental unit of the actin cytoskeleton. It is involved in a large number of cellular processes, including muscle contraction, lamellopodial extrusion, cell locomotion, cytokinesis, intracellular transport and cytoplasmic streaming. AD99, Actin protein that has been purified from bovine heart muscle by the method of Pardee and Spudich. Bovine cardiac actin is composed of 84% α-cardiac and 16%

Actins are highly conserved within the eukaryotic kingdom and exist in higher eukaryotes as multigene families. The different actin isoforms can show distinct cellular and sub-cellular expression and localization. It has been demonstrated that different isoforms have subtly different biochemical properties in vitro which supports functional diversity within isotypes in vivo. Monomeric actin (G-actin) can self assemble (polymerize) into microfilaments (F-actin), the fundamental unit of the actin cytoskeleton. It is involved in a large number of cellular processes, including muscle contraction, lamellopodial extrusion, cell locomotion, cytokinesis, intracellular transport and cytoplasmic streaming. AD99, Actin protein that has been purified from bovine heart muscle by the method of Pardee and Spudich. Bovine cardiac actin is composed of 84% α-cardiac and 16%

Actins are highly conserved within the eukaryotic kingdom and exist in higher eukaryotes as multigene families. The different actin isoforms can show distinct cellular and sub-cellular expression and localization. It has been demonstrated that different isoforms have subtly different biochemical properties in vitro which supports functional diversity within isotypes in vivo. Monomeric actin (G-actin) can self assemble (polymerize) into microfilaments (F-actin), the fundamental unit of the actin cytoskeleton. It is involved in a large number of cellular processes, including muscle contraction, lamellopodial extrusion, cell locomotion, cytokinesis, intracellular transport and cytoplasmic streaming. AKF99, Actin preformed filaments, with an average length of 8mM. AKF99 is formed from actin protein that has been purified from rabbit skeletal muscle by the method of Pardee and Spudich to greater than 99% purity. Skeletal muscle actin is composed of 99.5% α-actin and has an approximate mol

Actins are highly conserved within the eukaryotic kingdom and exist in higher eukaryotes as multigene families. The different actin isoforms can show distinct cellular and sub-cellular expression and localization. It has been demonstrated that different isoforms have subtly different biochemical properties in vitro which supports functional diversity within isotypes in vivo. Monomeric actin (G-actin) can self assemble (polymerize) into microfilaments (F-actin), the fundamental unit of the actin cytoskeleton. It is involved in a large number of cellular processes, including muscle contraction, lamellopodial extrusion, cell locomotion, cytokinesis, intracellular transport and cytoplasmic streaming. AKF99, Actin preformed filaments, with an average length of 8mM. AKF99 is formed from actin protein that has been purified from rabbit skeletal muscle by the method of Pardee and Spudich to greater than 99% purity. Skeletal muscle actin is composed of 99.5% α-actin and has an approximate mol

Actins are highly conserved within the eukaryotic kingdom and exist in higher eukaryotes as multigene families. The different actin isoforms can show distinct cellular and sub-cellular expression and localization. It has been demonstrated that different isoforms have subtly different biochemical properties in vitro which supports functional diversity within isotypes in vivo. Monomeric actin (G-actin) can self assemble (polymerize) into microfilaments (F-actin), the fundamental unit of the actin cytoskeleton. It is involved in a large number of cellular processes, including muscle contraction, lamellopodial extrusion, cell locomotion, cytokinesis, intracellular transport and cytoplasmic streaming. AKL95, Actin protein that has been purified from rabbit skeletal muscle by the method of Pardee and Spudich is between 95- 97% pure. Possible contaminants may include α-actinin (100 kDa), actin doublets (86 kDa) or Cap Z (33 kDa). Muscle actin has an approximate molecular weight of 43 kDa. A

Actins are highly conserved within the eukaryotic kingdom and exist in higher eukaryotes as multigene families. The different actin isoforms can show distinct cellular and sub-cellular expression and localization. It has been demonstrated that different isoforms have subtly different biochemical properties in vitro which supports functional diversity within isotypes in vivo. Monomeric actin (G-actin) can self assemble (polymerize) into microfilaments (F-actin), the fundamental unit of the actin cytoskeleton. It is involved in a large number of cellular processes, including muscle contraction, lamellopodial extrusion, cell locomotion, cytokinesis, intracellular transport and cytoplasmic streaming. AKL99, Actin protein that has been purified from rabbit skeletal muscle by the method of Pardee and Spudich is greater than 99% pure. Muscle actin has an approximate molecular weight of 43 kDa. Rabbit muscle actin is supplied as a white lyophilized powder. AKL99 can be used for identificatio