Results for Proteins & Peptides ( 111214 )
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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.
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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
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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
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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
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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.
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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
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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
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Purified rabbit muscle actin (Cat. # AKL99) has been modified to contain covalently linked pyrene at the cysteine 374 residue. An N-(1-pyrene) iodoacetamide is used to label the actin protein. Pyrene labeling stoichiometry has been determined to be 0.6 dyes per actin monomer. Pyrene labeled rabbit muscle actin has an approximate molecular weight of 43 kDa, and is supplied as a white lyophilized powder. The lyophilized protein is st able for 6 months when stored desiccated to <10% humidity at 4°C. The protein should be reconstituted to 20 mg/ml with distilled water; it will then be in the following buffer: 5 mM Tris-HCl pH 8.0, 0.2 mM CaCl2, 0.2 mM ATP, 5% sucrose, and 1% dextran. AP05 can be used for Studying actin polymerization in vitro and Studying the effects of actin binding proteins and drugs on actin polymerization in vitro.
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Purified rabbit muscle actin (Cat. # AKL99) has been modified to contain covalently linked pyrene at the cysteine 374 residue. An N-(1-pyrene) iodoacetamide is used to label the actin protein. Pyrene labeling stoichiometry has been determined to be 0.6 dyes per actin monomer. Pyrene labeled rabbit muscle actin has an approximate molecular weight of 43 kDa, and is supplied as a white lyophilized powder. The lyophilized protein is st able for 6 months when stored desiccated to <10% humidity at 4°C. The protein should be reconstituted to 20 mg/ml with distilled water; it will then be in the following buffer: 5 mM Tris-HCl pH 8.0, 0.2 mM CaCl2, 0.2 mM ATP, 5% sucrose, and 1% dextran. AP05 can be used for Studying actin polymerization in vitro and Studying the effects of actin binding proteins and drugs on actin polymerization in vitro.