Proteins & Peptides

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

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

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

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.

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.

APHL99, Non-muscle actin that has been purified from human platelets. The isotype composition of non-muscle actin is 85% β-actin and 15% γ-actin. Non-muscle actin has an approximate molecular weight of 43 kDa and is provided as a lyophilized white powder. Each unit of platelets used in the preparation of non-muscle actin has been found to be non-reactive by an FDA approved test for HBsAg, HBcAb, HIV-1/2 ab, HIV-1 RNA, HTLV I/II ab, HCV ab, HCV RNA, and syphilis. Each unit of platelets has been ALT tested with results less than an established cutoff. APHL99 can be used for identification and characterization of non-muscle actin binding proteins, in vitro actin polymerization studies, and antibody standard for Western blot analysis

APHL99, Non-muscle actin that has been purified from human platelets. The isotype composition of non-muscle actin is 85% β-actin and 15% γ-actin. Non-muscle actin has an approximate molecular weight of 43 kDa and is provided as a lyophilized white powder. Each unit of platelets used in the preparation of non-muscle actin has been found to be non-reactive by an FDA approved test for HBsAg, HBcAb, HIV-1/2 ab, HIV-1 RNA, HTLV I/II ab, HCV ab, HCV RNA, and syphilis. Each unit of platelets has been ALT tested with results less than an established cutoff. APHL99 can be used for identification and characterization of non-muscle actin binding proteins, in vitro actin polymerization studies, and antibody standard for Western blot analysis

APHL99, Non-muscle actin that has been purified from human platelets. Each unit of platelets used in the preparation of non-muscle actin has been found to be non-reactive by an FDA approved test for HBsAg, HBcAb, HIV-1/2 ab, HIV-1 RNA, HTLV I/II ab, HCV ab, HCV RNA, and syphilis. Each unit of platelets has been ALT tested with results less than an established cutoff. The isotype composition of non-muscle actin is 85% β-actin and 15% γ-actin. Non-muscle actin has an approximate molecular weight of 43 kDa and is provided as a lyophilized white powder. APHL99 can be used for identification and characterization of non-muscle actin binding proteins, in vitro actin polymerization studies, and antibody standard for Western blot analysis

Non-muscle actin purified from human platelets (Cat. # APHL99) has been modified to contain covalently linked rhodamine at random surface lysine residues. An activated ester of rhodamine is used to label the protein. The labeling stoichiometry has been determined to be 0.4 dyes per actin monomer. Rhodamine non-muscle actin has an approximate molecular weight of 43 kDa. Rhodamine non-muscle actin is supplied as a pink lyophilized powder. The lyophilized protein is stable for 6 months wh en stored desiccated to <10% humidity at 4°C. The protein should be reconstituted to 10 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. APHR can be used for In vivo actin polymerization studies (micro-injection into non-muscle cells) and In vitro motility studies using fluorescent F-actin and non-muscle myosins