Description: Vitronectin is a secreted glycoprotein that is synthesized in the liver. It circulates primarily in monomeric form, but can undergo conformational change to a structure that forms disulfide-linked multimers. The multimeric vitronectin can efficiently bind to, and incorporate into, the extracellular matrix. Within the matrix, vitronectin can support cell adhesion through binding to various integrins and other proteoglycans. Additionally, recombinant vitronectin can function as a chemically-defined matrix component in human embryonic stem cell renewal media. Recombinant Human Vitronectin is a 459 amino acid, single-chain, monomeric protein, which migrates at an apparent molecular weight of 75 kDa by SDS-PAGE under reducing conditions. The calculated molecular weight of Recombinant Human Vitronectin is 52.2 kDa.

Description: LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Murine LIF is a 19.9 kDa protein containing 180 amino acids residues, including three disulfide bonds.

Description: Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-β family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Description: LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Human LIF is a 19.7 kDa protein containing 180 amino acid residues, including three disulfide bonds.

Description: Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various in vivo models. Recombinant Human Leptin is a 16.0 kDa protein containing 147 amino acid residues.

Description: BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors, TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant Human soluble BAFF is a 152 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.