Proteins & Peptides

Interleukin-3 (IL-3) is a cytokine produced by activated T-cells and mast cells that is active on a broad range of hematopoietic cells and in the nervous system and appears to be important in several chronic inflammatory diseases. Recombinant Human IL-3 produced in E. coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15,000 Daltons.

Interleukin (IL)-4, secreted primarily by CD4(+) T cells is an immunomodulatory cytokine, which can inhibit the growth of tumour cells. IL-4 has been known as a Th2 cytokine and can act on B cells, T cells, and monocytes. Interleukin (IL)-4 exhibits antitumor activity in rodent experimental gliomas, which is likely mediated by the actions of IL-4 on a variety of immune cells present in and around the tumor masses. It participates in several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Recombinant Human IL-4 produced in E. coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 15,000 Daltons.

Interleukin 7 (IL-7), which is constitutively produced particularly by stromal cells from the bone marrow and thymus, plays a crucial role in T cell homeostasis. This cytokine is implicated in thymopoiesis because it sustains thymocyte proliferation and survival. It regulates peripheral naive T cell survival by modulating the expression of the anti-apoptotic molecule Bcl-2, and sustains peripheral T cell expansion in response to antigenic stimulation. Infection by the human immunodeficiency virus (HIV) leads to severe T lymphopenia and general immune dysfunction. Increased IL-7 plasma levels are generally observed in HIV-infected patients. IL-7 may also support bioenergetics that control cell fate decisions in lymphocytes. Recombinant Human IL-7 produced in E. coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17,412 Daltons.

Interleukin-2 (IL2) is a secreted immunomodulatory cytokine that is essential in regulation and proliferation of T and B lymphocytes, and other activities crucial to regulation of the immune response. The receptor of this cytokine (the IL-2R receptor) is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli. IL2 has been shown to have antitumor effects in some studies. This is probably mediated by cytotoxic effector cells. Produced by T-cells in response to antigenic or mitogenic stimulation, this protein can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural k

Interleukin (IL-9) is known to regulate many cell types involved in T- helper type 2 responses classically associated with asthma, including B- and T- lymphocytes, mast cells, eosinophils and epithelial cells. Growing evidence obtained from human genomic analysis and antigen-challenged transgenic mice suggests that IL-9 is a candidate factor in immunoglobulin E (IgE) production and thus is thought to be associated with bronchial inflammation and bronchial hyperresponsiveness (BHR). Recombinant Human IL-9 produced in E.coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14,004 Daltons.

Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as Tumor Angiogenesis Factor or Vascular Permeability 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 and vascular permeability it may play a role in stimulating vasolidation via nitric oxide-dependent pathways. 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 26 amino acids. Glycosylation is not required for efficient secretion of VEGF. Recombinant Human VEGF produced in E.coli is a double, non-glycosyl

Vascular endothelial growth factor-A was originally isolated from tumor cells and referred to as Tumor Angiogenesis Factor or Vascular Permeability 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 and vascular permeability it may play a role in stimulating vasolidation via nitric oxide-dependent pathways. 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 26 amino acids. Glycosylation is not required for efficient secretion of VEGF. Recombinant Human VEGF produced in E.coli is a double, non-glycosyl

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.