Proteins & Peptides

Granulocyte Macrophage Colony Stimulating Factor is produced in response to a number of inflammatory mediators by mesenchymal cells present in the hemopoietic environment and at peripheral sites of inflammation. Granulocyte Macrophage-CSF is able to stimulate the production of neutrophilic granulocytes, macrophages, and mixed granulocyte-macrophage colonies from bone marrow cells and can stimulate the formation of eosinophil colonies from fetal liver progenitor cells. GM-CSF can also stimulate some functional activities in mature granulocytes and macrophages. GM-CSF receptors shows significant homologies with other receptors for hematopoietic growth factors , including IL2-beta, IL-3 , IL -6 , IL-7 , EPO and the Prolactin receptors. Recombinant Human Granulocyte Macrophage CSF produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular weight of 14.5 kDa.

Granulocyte Macrophage Colony Stimulating Factor is produced in response to a number of inflammatory mediators by mesenchymal cells present in the hemopoietic environment and at peripheral sites of inflammation. Granulocyte Macrophage-CSF is able to stimulate the production of neutrophilic granulocytes, macrophages, and mixed granulocyte-macrophage colonies from bone marrow cells and can stimulate the formation of eosinophil colonies from fetal liver progenitor cells. GM-CSF can also stimulate some functional activities in mature granulocytes and macrophages. GM-CSF receptors shows significant homologies with other receptors for hematopoietic growth factors , including IL2-beta, IL-3 , IL -6 , IL-7 , EPO and the Prolactin receptors. Recombinant Human Granulocyte Macrophage CSF produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular weight of 14.5 kDa.

Recombinant Human Macrophage Inflammatory Protein-1 (CCL3, MIP-1) produced in E. coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Daltons.

Leptin inhibits food intake and stimulates energy expenditure. Leptin also has thermogenic actions and regulates enzymes of fatty acid oxidation. Severe hereditary obesity in rodents and humans is caused by defects in leptin production. In addition to its critical role in the physiologic regulation of body weight leptin has a variety of other physiologic and pathologic functions resembling those of cytokines. These functions include the regulation of hematopoiesis, angiogenesis, wound healing, inflammation, and immune responses. Leptin Human Recombinant produced in E. coli is a single, non-glycosylated, polypeptide chain containing 147 amino acids and having a molecular mass of 16 kDa.

SUMO3 is a member of the SUMO (small ubiquitin-like modifier) protein family which functions in a manner similar to ubiquitin. SUMO3 is bound to target proteins as part of a post-translational modification system and modifies numerous cellular proteins and affect their metabolism and function. SUMO3 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (1). SUMO3 predominantly detected in the cytoplasm (2). SUMO3 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Apoptosis/Autophagy, Cell Cycle, and NfkB Pathway research.

SUMO3 is a member of the SUMO (small ubiquitin-like modifier) protein family which functions in a manner similar to ubiquitin. SUMO3 is bound to target proteins as part of a post-translational modification system and modifies numerous cellular proteins and affect their metabolism and function. SUMO3 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (1). SUMO3 predominantly detected in the cytoplasm (2). SUMO3 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Apoptosis/Autophagy, Cell Cycle, and NfkB Pathway research.

Recombinant Human Interleukin-17-F is a non-glycosylated protein consisting of two 134 amino acid polypeptide chains that are cysteine linked homodimeric polypeptide chains with a molecular weight of 30 kDa. Homodimeric interleukin-17F is a member of the IL-17 family of six homodimeric proteins (IL-17A-17F). Activity studies reveal IL-17A to be the most potent, followed by IL-17A/F and IL-17F 100 fold lower than IL-17A.

Interleukin17-A is a proinflammatory cytokine produced by activated T cells and exists as a homodimer. This cytokine regulates the activities of NF-kappaB and mitogen-activated protein kinases. IL-17A can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of this cytokine are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis. IL17-A is the founding member of a group of cytokines called the IL-17 family. IL17-A was originally identified as a transcript from a rodent T-cell hybridoma. To elicit its functions, IL17 binds to a type I cell surface receptor called IL17R of which there are at least three variants: IL17RA, IL17RB, and IL17RC.

Human IL-32 alpha is one of approximately 6 splice variants of a gene cloned from the human lung carcinoma stable transfectant, A549-Rbeta. IL-32 alpha has been shown to induce IL-8, TNF-a, and MIP-2 production from human & mouse macrophage cell lines. It is upregulated in activated T- & NK-cells, and IFN-g-treated epithelial cells. Human recombinant IL-32 alpha produced in E. coli is a 131 amino acid non -glycosylated polypeptide with a molecular mass of 14.9 kDa.