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.

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.