"Peprotech"

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Osteoprotegerin (OPG) is a member of the TNFR superfamily that can act as a decoy receptor for RANKL. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilage. OPG is expressed in a wide variety of tissues, including the adult heart, lung, kidney, liver, spleen, prostate, lymph node, and bone marrow. OPG is secreted both as a monomeric and a dimeric protein. Its primary structure consists of seven distinct domains, four of which correspond to the extracellular cysteine-rich domains of TNFR proteins and constitute the soluble OPG. Recombinant Human OPG is a soluble 20.0 kDa protein containing 174 amino acid residues.

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Pleiotrophin and Midkine are structurally related heparin-binding neurotrophic factors, whose expression is developmentally regulated. The expression pattern of these neurotrophic factors suggests function in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm epithelial interaction. The expression of PTN increases during the process of brain embryogenesis, and reaches maximum levels at time of birth. The physiological roles of PTN and Midkine are largely unknown, but these neurotrophins have been implicated in the pathogenesis of neuroblastomas. Recombinant Human Pleiotrophin is a 15.4 kDa protein containing 136 amino acid residues and five intra-molecular disulfide bonds.

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Midkine (MK) and the functionally-related protein pleiotrophin are heparin-binding neurotrophic factors that signal through the same receptor, known as anaplastic lymphoma kinase (ALK). MK plays an important regulatory role in epithelial-mesenchymal interactions during fetal development and in postnatal lung development. MK chemoattracts embryonic neurons, neutrophils and macrophages, and exerts angiogenic, growth and survival activities during tumorigenesis. Recombinant Human Midkine is a 13.4 kDa protein containing 123 amino acid residues including five intra-molecular disulfide bonds.

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Artemin is a disulfide-linked homodimeric neurotrophic factor structurally related to GDNF, Artemin, Neurturin and Persephin. These proteins belong to the cysteine knot superfamily of growth factors that assume stable dimeric protein structures. Artemin, GDNF, Persephin and Neurturin all signal through a multicomponent receptor system, composed of RET (receptor tyrosine kinase) and one of the four GFRα (α1-α4) receptors. Artemin prefers the receptor GFRα3-RET, but will use other receptors as an alternative. Artemin supports the survival of all peripheral ganglia, such as sympathetic, neural crest and placodally-derived sensory neurons, and dopaminergic midbrain neurons. The functional human Artemin ligand is a disulfide-linked homodimer of two 12.0 kDa polypeptide monomers. Each monomer contains seven conserved cysteine residues, one of which is used for interchain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration. Recombinant Human Artemin is a 24.2 kDa, disulfide-linked homodimer formed by two identical 113 amino acid subunits.

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NNT-1/BCSF-3 is a neurotrophic factor with B-cell-stimulating capabilities. Expressed in the lymph nodes and spleen, NNT-1/BCSF-3 activates glycoprotein 130 (gp130) and leukemia inhibitory factor receptor member β (LIFR-β) by binding and inducing the tyrosine phosphorylation of, these receptors. In vitro , it supports the survival of chick embryo motor and sympathetic neurons. In mice, NNT-1/BCSF-3 induces serum amyloid A, causes body weight loss, and B-cell hyperplasia associated with increases in serum IgG and IgM. Recombinant Human NNT-1/BCSF-3 is a 22.4 kDa protein containing 199 amino acid residues.

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Resistin belongs to a family of tissue-specific cytokines termed FIZZ (found in inflammatory zones) and RELM. The four known members of this family, resistin, RELMα, RELMβ, and RELMγ, share a highly conserved C-terminal domain, characterized by 10 cysteine residues with a unique spacing motif of C-X11-C-X8-C-X-C-X3-C-X10-C-X-C-X-C-X9-C-C. Resistin is an adipose-derived cytokine (adipokine) whose physiological function and molecular targets are largely unknown. Studies have shown that resistin suppresses insulin's ability to stimulate glucose uptake, and postulated that resistin might be an important link between obesity and Type 2 diabetes. Other studies have indicated that resistin expression is severely suppressed in obesity, and that it may act as a feedback regulator of Adipogenesis. Recombinant Human Resistin is a 19.5 kDa, disulfide-linked, homodimeric protein composed of two identical 92 amino acid chains linked by a single disulfide bond.

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The gAcrp30 variant is a naturally occurring globular protein obtained by proteolytic processing of adiponectin. Adiponectin is produced and secreted exclusively by adipocytes, and is a relatively abundant plasma protein, accounting for up to 0.05% of total serum protein. Like Adiponectin, Acrp30 is capable of decreasing hyperglycemia and reversing insulin resistance. Additionally, gAcrp30 has been shown to be an important factor in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids (FFAs). The signaling receptors for adiponectin and gAcrp30 have recently been identified and named AdipoR1 and AdipoR2. AdipoR2 is predominantly expressed in the liver. This naturally occurring variant of Human gAcrp30/Adipolean is an 18.1 kDa protein, containing 14 extra amino acids extra at the N-terminus of human gAcrp30/Adipolean.

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GMF-β is a brain-specific protein that belongs to the actin-binding proteins ADF structural family. GMF-β appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines. Recombinant Human GMF-β is a 16.5 kDa globular protein containing 141 amino acid residues, including one intramolecular disulfide bond.

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Lectins, of either plant or animal origin, are carbohydrate-binding proteins that interact with glycoproteins and glycolipids on the surface of animal cells. The Galectins are lectins that recognize and interact with β-galactoside moieties. Galectin-3 regulates a number of biological processes, including embryogenesis, inflammatory responses, cell progression and metastasis. Galectin-3 is normally expressed in epithelia of a variety of tissues, including colon and endometrium, and in various inflammatory cells, including macrophages. Galectin-3 can function intracellularly, controlling the cell cycle and preventing T-cell apoptosis, and also extracellularly, by activating various cells, including monocytes/macrophages, mast cells, neutrophils, and lymphocytes. Expression of Galectin-3 is affected by neoplastic transformation, being up-regulated in certain types of lymphomas, and in thyroid and hepatic carcinomas. Conversely, it is down-regulated in other cancers such as colon, breast, ovarian, and uterine. Recombinant Human Galectin-3 is a globular 26.0 kDa protein containing 250 amino acid residues, but no disulfide bonds.

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Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, as they are frequently used in the analysis and production of proteins. Kex-2 cleaves at the carboxyl end of the recognition sequences Arg-Arg/X and Lys-Arg/X. Recombinant Yeast Kex-2 is a 60.4 kDa protease consisting of 558 amino acid residues.

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Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, as they are frequently used in the analysis and production of proteins. Glu-C cleaves at the Carboxyl side of E (can also cleave D under certain conditions). Recombinant Staphylococcus Glu-C is a 28.8 kDa protease consisting of 266 amino acid residues.

Supplier: Peprotech

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Furin is a calcium-dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa-(K/R)-R, where Xaa can be any amino acid. Recombinant Human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor, plus a C-terminal His-tag.

Supplier: Peprotech

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

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CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro . CNTF is also important for the survival of other neural cell types, including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant Rat CNTF is synthesized as a 199 amino acid polypeptide (22.7 kDa) lacking a hydrophobic N-terminal signal for secretion.

Supplier: Peprotech

GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional rat GDNF ligand is a disulfide-linked homodimer consisting of two 15 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Rat GDNF is 30.0 kDa.

Supplier: Peprotech

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Arg-C specifically cleaves at the carboxyl side of Arginine residues. Arg-C has a sulfhydryl requirement; it is activated by dithiothreitol, cysteine, or other sulfhydryl-containing reagents. The presence of calcium ions is essential. The enzyme is inhibited by oxidizing agents and sulfhydryl reactants, and by Co2+, Cu2+, Cd2+, and heavy metal ions. Recombinant Lysobacter Enzymogenes Arg-C is a 26.8 kDa protease consisting of 252 amino acid residues including a C-terminal His-Tag.