Proteins & Peptides

Regulated Upon Activation Normal T cell Express Sequence (RANTES), also called CCL5, is a chemokine produced by T cells three to five days after activation. RANTES is a promiscuous chemokine that signals through several G protein-coupled receptors, CCR5, CCR3, CCR1 and US28 (a viral receptor encoded by human CMV). The main function of RANTES is to recruit immune cells to the site of inflammation. Recombinant human RANTES is a non-glycosylated protein, containing 68 amino acids, with a molecular weight of 7.8 kDa.

Regulated Upon Activation Normal T cell Express Sequence (RANTES), also called CCL5, is a chemokine produced by T cells three to five days after activation. RANTES is a promiscuous chemokine that signals through several G protein-coupled receptors, CCR5, CCR3, CCR1 and US28 (a viral receptor encoded by human CMV). The main function of RANTES is to recruit immune cells to the site of inflammation. Recombinant human RANTES is a non-glycosylated protein, containing 68 amino acids, with a molecular weight of 7.8 kDa.

The MIP-3ß (also known as SCYA19) member of the intercrine beta (chemokine CC) family may play a role not only in inflammatory and immunological responses, but also in normal lymphocyte recirculation and homing. May play an important role in trafficking of T-cells in thymus, and T-cell and B-cell migration to secondary lymphoid organs. It is secreted. It specifically binds to chemokine receptor CCR7. MIP3ß is expressed at high levels in the lymph nodes, thymus and appendix, and at intermediate levels seen in colon and trachea, while low levels found in spleen, small intestine, lung, kidney and stomach. Recombinant Human MIP-3b produced in E. coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8809 Daltons. The recombinant protein shows potent chemotactic activity for T-cells and B-cells but not for granulocytes and monocytes.

The secreted cytokine RANKL (Receptor Activator of Nuclear factor kappa-B Ligand) is critically involved in osteoclastic differentiation and activation and in the regulation of specific immunity. RANKL exists as a homotrimer, is glycosylated, and occurs in 3 forms: cell-bound RANKL, which is expressed by osteoblast lineage cells, soluble RANKL (sRANKL), which is expressed by activated T lymphocytes, and a truncated ectodomain form derived from the cell-bound RANK Ligand, which is enzymatically processed by TACE (TNF-alpha converting enzyme (TACE; ADAM-17)). All three forms stimulate their specific receptor, RANK, which is located on osteoclastic and dendritic cells. RANKL binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. RANKL augments the ability of dendritic cells to stimulate naive T-cell proliferation. It may be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. It may also play

Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as Tumor Angiogenesis Factor. Although expressed at high levels in certain tumor-derived cells it is produced by a wide variety of cell types. In addition to stimulating vascular growth, vascular permeability, cell migration, and endothelial cell proliferation and growth, it may play a role in stimulating vasolidation via nitric oxide-dependent pathways and in inhibition of apoptosis. VEGF binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. Alternative splicing of the mRNA for VEGF-A results in several isoforms of the protein being produced. Rat and bovine VEGF are one amino acid shorter than the human factor, and the bovine and human sequences show a homology of 95 percent. In contrast to other factors mitogenic for endothelial cells such as FGF-1, FGF-2 and PDGF, VEGF is synthesized as a precursor containing a typical hydrophobic secretory signal sequence of

IL-29 (Interleukin-29) is a secreted cytokine with immunomodulatory activity. It may play a role in antiviral immunity. It up-regulates MHC class I antigen expression. IL-29 is a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IL28RA. The ligand/receptor complex seems to signal through the Jak-STAT pathway. Its induction is by viral infections or double stranded RNA. Recombinant IL-29 produced in E.coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19,895 Daltons.

EGF (Epidermal Growth Factor) protein, of the superfamily with the same name, is synthesized as a large precursor molecule that is proteolytically cleaved to generate the 53-amino acid epidermal growth factor peptide. This protein acts a potent mitogenic factor that plays an important role in the growth, proliferation and differentiation of numerous cell types. It is a magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. This protein acts by binding the high affinity cell surface receptor, epidermal growth factor receptor. Defects in this gene are the cause of hypomagnesemia type 4 (HOMG4). Dysregulation of this gene has been associated with the growth and progression of certain cancers. Alternate splicing results in multiple transcript variants. This protein exists in the membrane as a single-pass type I membrane protein, and contains 9 EGF-like domains as well as 9

BDNF is a member of the nerve growth factor family of trophic factors. In the brain BDNF has a trophic action on retinal, cholinergic, and dopaminergic neurons, and in the peripheral nervous system it acts on both motor and sensory neurons. Some protein domains of BDNF are identical with those of NGF and another neurotrophic factor, designated NT-3 (neurotrophin-3). It exists as monomers and homodimers, and binds to NTRK2/TRKB. Polyclonal antibodies raised against murine NGF have been shown to cross-react with both NT-3 and BDNF. The propeptide is N-glycosylated and glycosulfated. BDNF is converted into mature BDNF by plasmin (PLG). It is expressed in brain, and highly expressed in hippocampus, amygdala, cerebral cortex and cerebellum; it is also expressed in heart, lung, skeletal muscle, testis, prostate and placenta. Recombinant Human Brain-Derived Neurotrophic Factor produced in E.coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids and having

BDNF is a member of the nerve growth factor family of trophic factors. In the brain BDNF has a trophic action on retinal, cholinergic, and dopaminergic neurons, and in the peripheral nervous system it acts on both motor and sensory neurons. Some protein domains of BDNF are identical with those of NGF and another neurotrophic factor, designated NT-3 (neurotrophin-3). It exists as monomers and homodimers, and binds to NTRK2/TRKB. Polyclonal antibodies raised against murine NGF have been shown to cross-react with both NT-3 and BDNF. The propeptide is N-glycosylated and glycosulfated. BDNF is converted into mature BDNF by plasmin (PLG). It is expressed in brain, and highly expressed in hippocampus, amygdala, cerebral cortex and cerebellum; it is also expressed in heart, lung, skeletal muscle, testis, prostate and placenta. Recombinant Human Brain-Derived Neurotrophic Factor produced in E.coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids and having