6346 Results for: "Peprotech"

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Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant Human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).

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PlGF-1 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-1 is expressed in placental tissues, the colon, and mammary carcinomas. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. Recombinant Rat PlGF-1 is a 30.3 kDa disulfide-linked homodimeric protein of two 135 amino acid polypeptide chains.

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Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-1 is a 3.9 kDa protein containing 36 amino acid residues.

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Prolactin is a neuroendocrine hormone secreted by the pituitary gland. Its primary function is to promote and maintain lactation during pregnancy and suckling. In addition, prolactin plays an immunoegulatory role by stimulating the activities of ornithine decarboxylase and protein kinase C, which are important for the proliferation, differentiation, and function of lymphocytes. Recombinant Human Prolactin is a 23.0 kDa globular protein containing 200 amino acid residues.

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PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant Human PDGF-AB is a 26.4 kDa disulfide-linked dimer, consisting of one α chain and one β chain (234 total amino acids).

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TNFRI belongs to the TNFR superfamily of transmembrane proteins, and is expressed in most cell types. Binding of either TNF-α or TNF-β to TNFRI initiates a signal transduction pathway that results in the activation of the transduction factor NF-κB, whose target genes are involved in the regulation of inflammatory responses, and, in certain cells induce apoptosis. Soluble TNF Receptor I (sTNFRI) is capable of inhibiting TNF-α and TNF-β activities by acting as a decoy receptor that serves as a sink for the TNF ligands. The human TNFRI gene encodes for a 455 amino acid type I transmembrane protein, which contains a 21 amino acid signal sequence, a 190 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 221 amino acid cytoplasmic domain. Recombinant Human sTNF Receptor Type I is an 18.3 kDa protein (162 amino acid residues) comprising the cysteine-rich, ligand-binding portion of the extracellular domain of the TNFRI protein.

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OX40L, a member of the TNF superfamily of structurally related proteins, exists primarily as a type II membrane-bound, non-covalently linked, homotrimeric protein. It is expressed on antigen-presenting cells (APCs), such as dendritic cells and activated B-cells, as well as on various other cells such as vascular endothelial cells, mast cells, and natural killer cells. OX40L signals specifically through the OX40 receptor, which is expressed predominantly on CD4+ T cells, but also on certain activated CD8+ T cells. OX40/OX40L functions as a costimulatory signal, which is required for a productive interaction between antigen-presenting cells and their target T-cells. It enhances cell proliferation and survival, and increases expression of RANTES, IL-2, IL-3, and IFNγ. OX40/OX40L signaling plays an important role in immuno-regulatory communication, enabling the immune system to distinguish between “friend vs. foe” during activation; a mechanism typically termed immuno-tolerance. Recombinant Human sOX40 Ligand is a glycosylated 133 amino acid protein corresponding to the extracellular TNF homologous domain of the full length transmembrane protein. It migrates with an apparent molecular mass of 15.5 – 25.0 kDa on SDS-PAGE. Recombinant Human sOX40 Ligand has a calculated, theoretical molecular weight of 15.4 kDa.

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The Semphorins are a large family of phylogenetically conserved proteins that play a pivotal role in maintaining homeostasis in the immune system. Twenty members of this family have been identified and categorized into eight subclasses based on sequence similarity and distinctive structural features. CD100, also known as Sema4D, is a 150 kDa transmembrane class IV semaphorin. Studies have shown that CD100 can induce monocyte migration, T-cell activation, and B-cell survival, as well as T/B cell and T/DC “cooperation”. The CD100 precursor contains 862 amino acids, including a 21 a.a. signal sequence, a 713 a.a. extracellular domain, a 21 a.a. transmembrane sequence, and a 107 a.a. cytoplasmic region. The extracellular sequence contains several structural features, including a 479 a.a. “sema” domain, a 79 a.a. Ig-like sequence, and a 52 a.a. “Plexin-type repeat”. Recombinant Human sCD100 is a 78.9 kDa protein comprising the extracellular domain of CD100 (711 amino acids). SDS-PAGE analysis run under non-reducing conditions shows a mixture of disulfide linked dimer and monomer.

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LIGHT belongs to the TNF family of ligands, and can signal through the herpes virus entry mediator type A receptor (HVEM, TNFRSF14), LTβR, or bind to a decoy receptor, DcR3. It is expressed in splenocytes, activated PBL, CD8+ tumor infiltrating lymphocytes, granulocytes, and monocytes. LIGHT has the ability to active NF-κB, to co-stimulate the activation of lymphocytes and to induce apoptosis in certain human tumor cells. Recombinant Murine LIGHT is a 20.1 kDa protein containing 183 amino acid residues, comprising the TNF-homologous region of the LIGHT extracellular domain.

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Produced from sera of rabbits immunized with highly pure Recombinant Human IL-3. Anti­Human IL-3­specific antibody was purified by affinity chromatography employing an immobilized Human IL-3 matrix.

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Produced from sera of rabbits immunized with highly pure Recombinant Human IL-1α. Anti­Human IL-1α­specific antibody was purified by affinity chromatography employing an immobilized Human IL-1α matrix.

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Produced from sera of rabbits immunized with highly pure Recombinant Human IL-3. Anti­Human IL-3­specific antibody was purified by affinity chromatography and then biotinylated.

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Produced from sera of rabbits immunized with highly pure Recombinant Human RANTES (CCL5). Anti­Human RANTES (CCL5)­specific antibody was purified by affinity chromatography and then biotinylated.

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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 murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 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 Murine GDNF is 30.2 kDa.

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NT-4 is a neurotrophic factor structurally related to β-NGF, BDNF, and NT-3. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. NT-4 is expressed in the prostate, thymus, placenta, and skeletal muscle. NT-4 can signal through the LNGFR and trkB receptors, and promotes the survival of peripheral sensory sympathetic neurons. Recombinant Human NT-4 is a noncovalently linked homodimer of two 14.0 kDa polypeptide monomers (260 total amino acid residues).

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CDNF is a secreted neurotrophic factor that is expressed in brain, neuronal and certain non-neuronal tissues. It has been shown to promote survival, growth and function of dopamine-specific neurons. CDNF and its structural homolog, MANF, each contain an N-terminal saposin-like lipid binding domain, and a carboxyl-terminal domain, which is not homologous to previously characterized protein structures. CDNF and MANF can prevent 6-OHDA-induced degeneration of dopaminergic neurons by triggering survival pathways in a rat experimental model of Parkinson’s disease. Recombinant Human CDNF is an 18.5 kDa protein consisting of 162 amino acids, including 8 cysteine residues.

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Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-3 degrades fibronectin, laminin, collagens III, IV, and X, and cartilage proteoglycans. Recombinant Human MMP-3 is a 42.8 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids).

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NT-3 is a neurotrophic factor structurally related to β-NGF, BDNF, and NT-4.  These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures.  NT-3 is expressed by neurons of the central nervous systems, and can signal through the trk receptors.  NT-3 promotes the growth and survival of nerve and glial cells.  The amino acid sequences of human, murine and rat NT-3 are identical.  Recombinant Human NT-3 is a noncovalently linked homodimer of two 13.6 kDa polypeptide monomers (240 total amino acid residues). Manufactured using all Animal-Free reagents.

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IGF-BP3 is a 30 kDa, cysteine-rich secreted protein. It is the major IGF binding protein present in the plasma of human and animals, and it is also found in α-granules of platelets. In addition to its ability to modulate the activity of IGF-I and IGF-II, IGF-BP3 exerts inhibitory effects on follicle stimulating hormone (FSH) activity. Decreased plasma levels of IGF-BP3 often results in dwarfism, whereas elevated levels of IGF-BP3 may lead to acromegaly. The expression of IGF-BP3 in fibroblasts is stimulated by mitogenic growth factors, such as Bombesin, Vasopressin, PDGF, and EGF. Recombinant Human IGF-BP3 is a 28.8 kDa protein consisting of 264 amino acid residues.

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Animal-Free Murine IL-22 Recombinant Protein, Purity: >98%, Source: E.coli, Biological Activity: By its ability to induce IL-10 secretion in COLO 205 (human colon carcinoma cells), Synonyms: Interleukin-

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Human HPRG Recombinant Protein, Purity: >90%, Source: CHO cells, Biological Activity: Measured by its ability to support adhesion of Con-A activated MOLT-4 cells to the Recombinant Human HPRG-coated surface, Synonyms: H

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Produced from sera of rabbits immunized with highly pure Recombinant Human NT-3. Anti­Human NT-3­specific antibody was purified by affinity chromatography employing an immobilized Human NT-3 matrix.

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The Murine Hematopoietic Stem Cell Expansion Cytokine Package contains the key components required for ex vivo mouse hematopoietic stem cells.

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CD40, a member of the TNF receptor superfamily, is a cell surface protein expressed on B cells, dendritic cells, monocytes, thymic epithelial cells and, at low levels, on T cells.  Signaling though CD40 plays an important role in the proliferation and differentiation of B cells, and is critical for immunoglobulin (Ig) class switching.  The membrane-anchored CD40-Ligand is expressed almost exclusively on activated CD4+ T lymphocytes.  Failure to express CD40L leads to “immunodeficiency with hyper-IgM”, a disease characterized by failure to produce IgG, IgA and IgE.  The human CD40L gene codes for a 261 amino acid type II transmembrane protein, which contains a 22 amino acid cytoplasmic domain, a 24 amino acid transmembrane domain, and a 215 amino acid extracellular domain.  The soluble form of CD40L is an 18 kDa protein comprising the entire TNF homologous region of CD40L and is generated in vivo by an intracellular proteolytic processing of the full length CD40L.  Recombinant Human soluble CD40 ligand is a 16.3 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L. Manufactured using all Animal-Free reagents.

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PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant Murine PDGF-AA is a 28.7 kDa disulfide-linked homodimer of two α chains (250 total amino acids).

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M-CSF is a potent hematopoietic factor produced by a variety of cells, including lymphocytes, monocytes, fibroblasts, endothelial cells, myoblasts and osteoblasts. It is a key regulator of cellular proliferation, differentiation, and survival for blood monocytes, tissue macrophages, and their respective progenitor cells. M-CSF has been shown to play important roles in modulating dermal thickness and fertility. M-CSF is clinically used in the treatment of infection, malignancies and atherosclerosis. It facilitates hematopoietic recovery after bone marrow transplantation. Human M-CSF is reactive in murine systems, but the murine molecule exhibits no activity on human cells. Recombinant Murine M-CSF is a 36.4 kDa homodimeric protein consisting of two 156 amino acid polypeptide subunits.

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MIP-3α is a CC chemokine, expressed in the liver, lymph nodes, appendix, PBL and lungs that can signal through the CCR6 receptor. MIP-3α is chemotactic towards lymphocytes and dendritic cells. Additionally, it promotes the adhesion of memory CD4+ T cells, and inhibits colony formation of bone marrow myeloid immature progenitors. Recombinant Human MIP-3α (CCL20) is an 8.0 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

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IFN λ1, 2, and 3 (also known as IL-29, IL-28A and IL-28B respectively) are distantly related to the IL-10 family and the interferons. All three IFN-lambdas use a distinct receptor system composed of an IFN-λR1 subunit (also called CRF2-12) and IL-10R2 subunit (also called CRF2-14). Signaling through this receptor system induces antiviral defenses similar to, but distinct from, that of type I interferons. Recombinant Human IFN-λ1 is a 19.8 kDa protein containing 178 amino acid residues.

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SCF is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. The human SCF gene encodes for a 273 amino acid transmembrane protein, which contains a 25 amino acid N-terminal signal sequence, a 189 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 36 amino acid cytoplasmic domain. The secreted soluble form of SCF is generated by proteolytic processing of the membrane anchored precursor. Recombinant Human SCF is an 18.4 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.

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MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor, and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines, including the four highly conserved cysteine residues present in CC chemokines. Recombinant Human MEC (CCL28) is a 12.3 kDa protein containing 108 amino acid residues.