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Description: The MCP proteins are members of the CC chemokine family that signal through CCR2 and, with the exception of MCP-1, other CCR receptors. The MCP proteins chemoattract and activate monocytes, activated T cells, basophils, NK cells, and immature dendritic cells. The MCP family cross-reacts across species. Recombinant Murine MCP-3 (CCL7) is an 8.5 kDa protein containing 74 amino acid residues including the four highly conserved cysteine residues present in the CC chemokines.

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Description: GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is the stimulation of pancreatic β cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include the suppression of plasma glucagon levels, inhibition of gastric motility, and promotion of satiety. The secretion of GLP-1 from intestinal L cells is stimulated by nutrients, hormones, and neural inputs. On the other hand, insulin has been reported to inhibit GLP-1 release, indicating that a feedback loop mechanism regulates GLP-1 secretion. In addition to being the precursor of GLP-1, proglucagon, whose primary structure is highly conserved in mammalian species, is also the precursor for other members of the glucagon family of peptide hormones, including glicentin-related pancreatic peptide (GRPP), glucagons, and GLP-2. Recombinant Human GLP-1 is a 3.3 kDa polypeptide consisting of 31 amino acid residues.

Catalog Number: (10781-760)

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Description: 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 Rat M-CSF is a 36.2 kDa homodimeric protein consisting of two 155 amino acid polypeptide subunits.

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Description: Thrombomodulin (TM, CD141, THBD) is an endothelial cell-expressed, transmembrane glycoprotein that can form a complex with the coagulation factor, thrombin. The thrombomodulin/thrombin complex converts protein C to its activated form, protein Ca, which in turn proteolytically cleaves and deactivates factor Va and factor VIIIa, two essential components of the coagulation mechanism. This inactivation reduces the generation of additional thrombin, and thereby effectively prevents continued coagulation. Reduced levels of thrombomodulin can correlate with the pathogenesis of certain cardiovascular diseases, such as atherosclerosis and thrombosis. However, the serum levels of the truncated circulating form of thrombomodulin are typically elevated during inflammation and in the presence of various inflammatory-related diseases. The thrombomodulin protein contains 575 amino acids, including an 18 a.a. signal sequence, a 497 a.a. extracellular domain, a 24 a.a. transmembrane sequence, and a 36 a.a. cytoplasmic region. Recombinant Human Thrombomodulin is a 51.4 kDa, 491-amino-acid length glycoprotein containing the extracellular domain of thrombomodulin.

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Description: Vimentin is a class III intermediate filament protein predominantly found in cells of mesenchymal origins, such as vascular endothelium and blood cells, where it functions as a major cytoskeletal component. Due to its importance and abundance in the cytoskeletal structure of mesenchymally-derived cells, vimentin is frequently used as a developmental marker within cells of mesenchymal origin or cells undergoing epithelial-mesenchymal transition, which can occur during both normal and metastatic growth. An active participant within several critical processes of cellular organization and protein regulation, vimentin is involved in the anchorage of organelles within the cytoplasmic matrix, development of astrocytes, and the disassembly of cellular components during the execution phase of apoptosis. Abnormalities in the normal physiological pathways of vimentin have been implicated in deficient motility and directional migration involved in wound healing, cellular growth and development, as well as the adhesion-site accumulation of vimentin on lens epithelial cells in cases of dominant cataracts. Recombinant Human Vimentin is a 54.3 kDa protein consisting of 471 amino acid residues, including a 6-residue C-terminal His-Tag.

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Description: FGF-10 is a heparin-binding growth factor that belongs to the FGF family.

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Description: ENA-78 is a CXC chemokine that signals through the CXCR2 receptor. It is expressed in monocytes, platelets, endothelial cells, and mast cells. ENA-78 is a chemoattractant for neutrophils. The three naturally occurring variants of human ENA-78; ENA 5-78, ENA 9-78 and ENA 10-78, contain 74, 70, and 69 amino acid residues, respectively, and possess the same biological activity. ENA-78 contains the four conserved cysteine residues present in CXC chemokines, and also contains the ‘ELR’ motif common to CXC chemokine that bind to the CXCR1 and CXCR2 receptors. Recombinant Human ENA-78 (CXCL5) is an 8.0 kDa protein consisting of 74 amino acid residues.

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Description: Macrophage migration inhibitory factor (MIF) is a small secreted protein that can act as a pleiotropic pro-inflammatory cytokine, as well as an enzyme. MIF pro-inflammatory activity can be initiated by signaling through CD74 and CD44, resulting in the secretion of TNF-a, IL-1, IL-6, IL-8, and variousmMPs. The enzymatic activity of MIF is characterized by its ability to act as a tautomerase, capable of catalyzing the keto-to-enol isomerization of keto-phenylpyruvate and L-dopachrome. It appears as though MIF catalytic activity is dependent upon a trimeric configuration and a free N-terminal proline residue. Insect cell-derived Recombinant Human MIF is a 15 kDa protein containing 124 amino acid residues, including an N-terminal His-tag.

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Description: 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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Description: Recombinant Human sIL-6 Receptor A, Purity: Greater than 95% by SDS-PAGE gel and HPLC analyses, Source: CHO cells, Determined by its ability to intensify the IL-6 induced growth inhibition, Synonyms: soluble IL-6 receptor alpha, CD126, Size: 1MG

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Description: Human soluble DLL-1 comprises the extracellular signaling domain of DLL-1, a member of the Delta/Serrate/Lag-2 (DSL) family of single-pass type I trans-membrane proteins that serve as ligands for Notch receptors. It is expressed primarily in the heart, pancreas and epidermis. DLL-1 functions to specifically activate the Notch-1 and Notch-2 receptors. Proteolytic cleavage of DLL-1 produces a secreted extracellular domain, sDLL-1, that interacts with Notch receptors expressed on adjacent cells. Notch signaling plays an essential role in controlling cell fate decisions during prenatal development and postnatal stem cell renewal, and differentiation in many tissues. Human sDLL-1 blocks monocyte differentiation into macrophages, but permits differentiation into dendritic cells. In hematopoietic progenitor cells, hsDLL-1, suppresses differentiation into B-cells, while promoting differentiation into T-cells and NK cell precursors. In cell culture, human sDLL-1 has been shown to promote expansion of hematopoietic progenitor cells and suppress apoptosis by inhibiting differentiation. Overexpression of Notch receptors appears to inhibit differentiation in several mammalian cell lines, and increasing evidence suggests that Notch signaling is frequently downregulated in human malignancies. The human DLL-1 gene consists of a 528 amino acid extracellular domain with one DSL domain, eight EGF-like repeats, a 23 amino acid transmembrane domain, and a 155 amino acid cytoplasmic domain. The calculated molecular weight of Recombinant Human sDLL-1 is 56.3 kDa.

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Description: 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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Description: Myostatin is a TGF-β family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond.

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Description: 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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Description: Recombinant Human/Murine/Rat Irisin, Purity: Greater than 90% by SDS-PAGE, Source: CHO cells, Cross Reactivity: Human, Mouse, Rat, Synonyms: Fibronectin type III domain-containing protein 5, Fibronectin type III repeat-containing protein 2, Size: 500UG

Catalog Number: (76303-880)

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Description: 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-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens. Recombinant Human MMP-1 is a 42.7 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain, which is involved in substrate specificity, and in binding TIMP-1.