Proteins & Peptides

Recombinant Human Placental Lactogen

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.

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

T240, Tubulin protein has been purified from porcine brain by an adaptation of the method of Shelanski et al. Further purification was achieved by cation exchange chromatography. Tubulin consists of a heterodimer of one alpha and one beta isotype, each tubulin isotype is 55 kDa in size, SDS-PAGE analysis shows tubulin running as a 55 kDa species. Typically, the molar equivalent of tubulin is defined as the heterodimer which has a molecular weight of 110 kDa. The protein is supplied as a white solid. Protein purity was determined to be >99%. The recommended storage conditions for the lyophilized material is desiccated at 4°C. Under these conditions the protein is stable for 1 year. Lyophilized protein can also be stored desiccated at -70°C. Applications for T240 include, IC50 & EC50 determinations for anti-tubulin ligands, and Characterization of tubulin binding proteins.

T333P, Tubulin protein has been purified from porcine brain by an adaptation of the method of Shelanski et al. The tubulin protein has been covalently linked to a long-chain biotin derivative on random surface lysines. An activated ester of the biotin derivative is used in the labeling procedure. A long-chain biotin derivative was selected for this procedure because it allows the biotin molecules to be spaced far enough away from the tubulin protein so as not to interfere with subsequent detection techniques, e.g. binding to streptavidin based reagents and beads. The labeling stoichiometry was determined to be approximately 1 to 2 biotins per tubulin heterodimer. Biotin-labeled tubulin is supplied as a white lyophilized powder. The recommended storage conditions for the lyophilized material is 4°C and <10% humidity. Under these conditions the protein is stable for 6 months. Lyophilized protein can also be stored desiccated at -70°C for 5 months. Biotin tubulin can be bound to

Porcine brain tubulin (>99% pure, see Cat. # T240) has been modified to contain covalently linked HiLyte Fluor™ 488 (HiLyte Fluor is a trademark of Anaspec Inc, CA) at random surface lysines. An activated ester of HiLyte Fluor™ 488 was used to label the protein. HiLyte Fluor™ 488 tubulin is in a versatile, stable and easily shipped format. It is ready for micro-injection or in vitro polymerization. Cytoskeleton, Inc. also offers AMCA (Cat. # TL440M), rhodamine (Cat. # TL590M), X-rhodamine (Cat. # TL620M) and HiLyte Fluor™ 647 (Cat. # TL670M) labeled tubulins of the same quality. Applications for TL488M include : Laser based applications, Monitoring microtubule dynamcs in living cells, Speckle microscopy, Formation of fluorescent microtubules, Microscopy studies of MAP and microtubule associated motor activities, and Nanotechnology

This peptide is derived from the C-terminus of the chemokine, complement fragment 5 anaphylatoxin (C5a). This peptide functions as a C5a receptor agonist. C5a is a plasma protein involved in cellular inflammatory processes by inducing chemotaxis, degranulation of leukocytes, increased vascular permeability, and cytokine production. The cyclohexylalanine at position 5 is crucial to agonist function. Arg at the last position is of the d-isomer.

This heparin-binding peptide is derived from vitronectin (367-378). Vitronectin is a glycoprotein found in monomer form in the blood and oligomer form in the extraceullular matrix. This peptide has been shown to promote the adhesion and undifferentiated growth of human pluripotent stem cells.

Universal Type I IFN-Alpha is a unique hybrid interferon constructed from recombinant human interferons alpha A and alpha D (Human IFN-Alpha A/D [BglII]). Activity has been observed on many mammalian cells, including human, monkey, mouse, bovine, rat, cat, pig, rabbit, guinea pig, or hamster. This product is useful for cross-species testing with interferon or for species where autologous interferon is not available. Crucial for cross-species comparative studies in virology, immune modulation, and more.