"peptide synthesis"

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Interleukin-1 Receptor Antagonist (IL-1RN) is a member of the IL-1 family. Endogenous IL-1RN is produced in numerous animal disease models as well as in human autoimmune and chronic inflammatory diseases. It binds to IL-1 receptors in competition with IL-1, but does not elicit intracellular response from this binding. Its role in counteracting the proinflammatory effects of IL-1 is being studied by numerous research groups. IL-4 and IL-13 have been shown to amplify the stimulatory effect of IL1-beta on the production of soluble and intracellular forms of IL-1RN. The regulated expression of IL-1RN in various cell types has been shown to be influenced by cytokines. In synovial fibroblasts, IL-1, TNF-alpha, or PDGF markedly enhances the synthesis of IL-1RN.

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Human epidermal growth factor receptor 2 (HER2) is a type of membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 plays a key role in development, cell proliferation and differentiation. HER2 has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on. HER2 is activated by dimerization and not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.It is heterodimer with EGFR, ERBB3 and ERBB4. HER2 associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. It implicated in transcriptional activation of CDKN1A and the function of the protein involves STAT3 and SRC. And also it involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.

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LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities also include the induction of hematopoietic differentiation in normal and myeloid leukaemia cells, the induction of neuronal cell differentiation and the stimulation of acute-phase protein synthesis in hepatocytes. LIF activates JAK & STAT signalling in human embryonic stem (ES) cells, but this pathway does not maintain pluripotency in these cells, which instead rely on FGF2-mediated ERK signalling. By contrast, mouse ES cells can be maintained by LIF-mediated JAK & STAT signalling. LIF binds to a high affinity heterodimeric receptor complex consisting of two proteins: LIF-R alpha that binds LIF with low affinity and the 130kDa (gp130) subunit that by itself does not bind LIF, but is required for high affinity binding of LIF.

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ITIH3, which is short for Inter-alpha-trypsin inhibitor heavy chain H3, is a 890 aa. protein. It is secreted expression, and belongs to the ITIH family. I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin. ITTH3 may act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localisation, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes.

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EGF is a single-pass type I membrane protein,containing 8 LDL-receptor class B repeats and 9 EGF-like domains. EGF results in cellular proliferation, differentiation, and survival.EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.

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Mouse Vascular endothelial growth factor (VEGF or VEGF­A), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. It is a member of the PDGF/VEGF growth factor family that is characterized by a cystine knot structure formed by eight conserved cysteine residues. Alternately spliced isoforms of 120, 164 and 188 aa found in mouse. VEGF binds the type I transmembrane receptor tyrosine kinases VEGF R1 (also called Flt­1) and VEGF R2 (Flk­/KDR) on endothelial cells.Although affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity. VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells.It may play a role in increasing vascular permeability during lactation, when increased transport of molecules from the blood is required for efficient milk protein synthesis.

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MHC Class I Polypeptide-Related Sequence A (MICA) is a transmembrane glycoprotein that functions as a ligand for human NKG2D. Unlike classical MHC class I molecules, MICA does not form a heterodimer with beta-2-microglobulin. MICA shares 85% amino acid identity with a closely related protein, MICB. MICA acts as a stress-induced self-antigen that is recognized by NK cells, NKT cells, and most of the subtypes of T cells. As a Ligand for the KLRK1/NKG2D receptor, MICA binds to KLRK1 leads to cell lysis. MICA functions as an antigen for gamma delta T cells and is frequently expressed in epithelial tumors. MICA antigens are able to elicit the synthesis of alloantibodies in transplant recipients. Studies have shown that anti-MICA antibodies are associated with acute renal allograft rejection and failure. MICA recognition is involved in tumor surveillance, viral infections, and autoimmune diseases.

Supplier: Stemcell Technologies

Midkine is a member of a unique family of heparin-binding growth factors that are structurally different from other fibroblast growth factors (Muramatsu; Takada et al.). Midkine is a proinflammatory cytokine, promoting the migration of leukocytes, fibrinolysis, and acting as a chemotactic agent towards neutrophils (Muramatsu; Said et al.; Takada et al.). It also regulates growth, differentiation, and development during the midgestion stage of embryogenesis, and promotes angiogenesis (Muramatsu; Said et al.; Takada et al.). The protein structure consists of three antiparallel β-sheets and is highly conserved between species (Muramatsu; Takada et al.). While the exact signal pathway is not known, proposed pathways include promoting LRP, inhibiting Src kinase, activating paxillin and STAT1α, activating PI2 and MAP kinases, suppressing caspases, binding to α6β1-integrin and tetraspanin, activating FAK, phosphorylating STAT3, suppressing STAT5 phosphorylation, activating ALK, activating PI3 kinase and transcription of NFkB, binding to neuroglycan C or nucleolin, and binding to eIF3 (Muramatsu). In cultured cells, midkine influences growth and survival of neural precursor cells, synthesis of cytokines from endothelial and renal epithelial cells, and promotes synthesis of extracellular matrices from fibroblasts (Muramatsu; Takada et al.).

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Bone morphogenetic protein 2 (BMP-2) is a member of the BMP subgroup of the TGF-beta superfamily. It plays a dominant role in embryonic dorsalventral patterning, organogenesis, limb bud formation and bone formation and regeneration. BMP-2 signals through heterodimeric complexes composed of a type I receptor (Activin RI, BMP-RIA or BMP-RIB) and a type II receptor (BMP-RII or Activin RIIB). BMP-2 induces chondrocyte proliferation, endochondral bone formation, longitudinal bone growth and bone and cartilage repair. It induces ectopic bone formation or calcification by promoting osteogenic and chondrogenic differentiation in mesenchymal cells, stem cells and vascular smooth muscle cells. It also promotes the maintenance and repair of colonic epithelium, suppresses neuronal dopamine synthesis and release, induces apoptosis in medulloblastoma cells and is required for cardiac contractility.

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The three mammalian isoforms of TGF-β, TGF-β1, β2, β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes including embryogenesis, tissue remodeling and would healing. They are secreted predominantly as latent complexes which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and /or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-β3 is still unknown but its expression pattern suggests a role in the regulation of certain development processes. Recombinant TGF-β3 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.Manufactured using all non-animal reagents.

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Lipocalin-2 (LCN2) is also known as oncogene 24p3 or neutrophil gelatinase-associated lipocalin (NGAL), MSFI, The binding of lipocalin-2 to bacterial siderophores is important in the innate immune response to bacterial infection. Upon encountering invading bacteria the toll-like receptors on immune cells stimulate the synthesis and secretion of lipocalin-2. Secreted lipocalin-2 then limits bacterial growth by sequestering iron-containing siderophores. Lipocalin-2 also functions as a growth factor. LCN2 is strongly upregulated during inflammation and is upregulated by interleukin 1 (but not TNF alpha) in humans. There are indications that some forms of acne could be caused due to the gene not being transcribed, and that Isotretinoin corrects this. NFAT3 (NFATc4)NFAT by blocking the expression of LCN2 inhibits breast carcinoma cell motility. Recent studies have revealed that NGAL plays an important role in the physiopathology of chronic myeloid leukaemia (CML) mediated by BCR-ABL.

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GFER is a hepatotrophic growth factor and flavin-linked sulfhydryl oxidase which belongs to the Erv1/ALR family of proteins. GFER is widely expressed in various human tissues. They are two isoforms of this protein. Isoform 1 could regenerate the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen. Isoform 2 may act as an autocrine hepatotrophic growth factor promoting liver regeneration. GFER could also induce the expression of S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases (ODC). S-adenosylmethionine decarboxyl-ase and ornithine decarboxylases play an important role in the synthesis of polyamines.

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils, and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation, and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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Serpin A1 is also known as Alpha-1-antitrypsin (A1AT), serum trypsin inhibitor, alpha-1 proteinase inhibitor (A1PI), AAT, which belongs to the serpin family. Most serpins inactivate enzymes by binding to them covalently, requiring very high levels to perform their function. Like all serine protease inhibitors, A1AT has a characteristic secondary structure of beta sheets and alpha helices. Serpin A1 / A1AT is inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form of SerpinA1 inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin. Serpin A1 / A1AT protects tissues from enzymes of inflammatory cells, especially neutrophil elastase. Defects in SERPINA1 are the cause of alpha-1-antitrypsin deficiency (A1ATD).