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Supplier: PeproTech, Inc.

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 Rat MCP-1 (CCL2) is a 14.0 kDa protein containing 125 amino acid residues, including the four highly conserved cysteine residues present in the CC chemokines.

Supplier: PeproTech, Inc.

Description: Relaxin-3 is a secreted protein structurally related to insulin that is expressed primarily in the brain and central nervous system. Relaxin-3 has been identified as the ligand for the GPCR135 receptor, previously known as “somatostatin-like” or “angiotensin-like” peptide receptor, and has also been identified for binding specifically to the LGR7 receptor, previously identified as an “orphan” G protein-coupled receptor. Signaling by relaxin-3 through its target receptors is, most likely, part of a CNS processing system, activated in response to signaling by neuropeptides and other factors. Intracerebroventricular injections of relaxin-3 have been shown to cause a significant increase of food intake and body weight in Wistar rats. Recombinant Human Relaxin-3 is a 5.5 kDa, disulfide-linked, heterodimeric protein consisting of a 24 amino acid A-chain and a 27 amino acid B-chain.

Supplier: PeproTech, Inc.

Description: IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Human IL-2 is a 15.5 kDa protein, containing 134 amino acid residues including one intrachain disulfide bond.

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Supplier: PeproTech, Inc.

Description: HB-EGF is an EGF-related growth factor that signals through the EGF receptor, and stimulates the proliferation of smooth muscle cells (SMC), fibroblasts, epithelial cells, and keratinocytes. HB-EGF is expressed in numerous cell types and tissues, including vascular endothelial cells, and vascular SMC, macrophages, skeletal muscle, keratinocytes, and certain tumor cells. The ability of HB-EGF to specifically bind heparin and heparin sulfate proteoglycans is distinct from other EGF-like molecules, and may be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells. The human HB-EGF gene encodes a 208 amino acid transmembrane protein, which can be proteolytically cleaved to produce soluble HB-EGF. Recombinant Human HB-EGF is a 9.7 kDa protein containing 86 amino acid residues, corresponding to the extracellular EGF-like and heparin-binding domains of the full length HB-EGF protein.

Supplier: PeproTech, Inc.

Description: Oncostatin M (OSM) is a growth and differentiation factor that participates in the regulation of neurogenesis, osteogenesis and hematopoiesis. Produced by activated T cells, monocytes and Kaposi’s sarcoma cells, OSM can exert both stimulatory and inhibitory effects on cell proliferation. It stimulates the proliferation of fibroblasts, smooth muscle cells and Kaposi’s sarcoma cells, but inhibits the growth of some normal and tumor cell lines. It also promotes cytokine release (e.g. IL-6, GM-CSF and G-CSF) from endothelial cells, and enhances the expression of low-density lipoprotein receptors in hepatoma cells. OSM shares several structural and functional characteristics with LIF, IL-6, and CNTF. Human OSM is active on murine cells. The human OSM gene encodes for a 252 amino acid polypeptide, containing 25 amino acid signal sequence for secretion and a 227 precursor protein. Proteolytic processing of this precursor removes an 18 amino acid C-terminal peptide, and generates the mature OSM form. Recombinant Human Oncostatin M is a 23.6 kDa protein, containing 209 amino acid residues.

Supplier: PeproTech, Inc.

Description: BMPs (Bone Morphogenetic Proteins) belong to the TGF-β superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with an osteoconductive carrier such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 appears to play an important role in cardiac morphogenesis, and is expressed in a variety of other tissues, including lung, liver, spleen, prostate, ovary, and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains (monomers) linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant Human/Murine/Rat BMP-2 derived from

Supplier: PeproTech, Inc.

Description: SDF-1α and β are stromal-derived, CXC chemokines that signal through the CXCR4 receptor. SDF-1α and β chemoattract B and T cells, and have been shown to induce migration of CD34+ stem cells. Additionally, the SDF-1 proteins exert HIV-suppressive activity in cells expressing the CXCR4 receptor. Human and murine SDF-1 proteins act across species. SDF-1α and β contain the four highly conserved cysteine residues present in CXC chemokines. The mature SDF-1β protein, produced by an N-terminal truncation of two additional amino acids, after removal of the signal sequence, contains 72 amino acid residues. Recombinant Murine SDF-1β (CXCL12) is an 8.5 kDa protein containing 72 amino acid residues.

Supplier: PeproTech, Inc.

Description: IL-1α is a non-secreted, proinflammatory cytokine produced in a variety of cells, including monocytes, tissue macrophages, keratinocytes, and other epithelial cells. Both IL-1α and IL-1β bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities including the stimulation of thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, mitogenic FGF-like activity, and the release of prostaglandin and collagenase from synovial cells. However, whereas IL-1β is a secreted cytokine, IL-1α is predominantly a cell-associated cytokine. Recombinant Rat IL-1α is a 17.7 kDa protein containing 155 amino acid residues.

Supplier: PeproTech, Inc.

Description: RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic cells. These dendritic cells then stimulate naive T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK+ T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells,including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. 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. Human RANKL is reactive on murine cells. PeproTech's CHO cell-derived Recombinant Human sRANK Ligand is a 22.1 kDa polypeptide comprised of the TNF-homologous region of RANKL and a N-terminal His-tag.

Supplier: PeproTech, Inc.

Description: Programmed cell death protein 1 (PD-1), or CD279, is a type I inhibitory transmembrane receptor of the CD28 receptor family that, along with its B7 family ligands, programmed death ligand 1 (PD-L1) and programmed death ligand 2 (PD-L2), belongs to the immunoglobulin superfamily. While other CD28 family members are expressed predominantly in T cells, PD-1 is widely expressed and found in multiple lymphocytes including T cells, B cells, myeloid, and NKT cells upon activation. PD-1 is a negative regulator of immune response, and is referred to as an inhibitory immune checkpoint molecule. Ligation with PD-L1 or PD-L2 results in inhibited activation, proliferation, and cytokine secretion (e.g. IFN-gamma, IL-10) in T cells, ultimately dampening immune response. Despite the strong homology between PD-L1 and PD-L2, each ligand appears to display distinct lymphokine expression patterns and potency. Blockage of PD-1 ligation by monoclonal antibodies has been proven to be an effective anti-tumor treatment by allowing the immune response to remain active and attack the tumorigenic cells that otherwise would have escaped detection. PD-1 and its ligands have been implicated in numerous autoimmune diseases, inflammatory liver disease and cancers. The naturally occurring human PD-1 monomer consists of a 150 amino acid extracellular domain, a 21 amino acid transmembrane domain, and a 97 amino acid cytoplasmic domain. PeproTech's CHO cell-derived Recombinant Human PD-1 Fc is a glycosylated, disulfide-linked homodimer of 501 amino acid residues whose monomer consists of the 268-amino-acid length mature PD-1 sequence fused to the 231-amino-acid length Fc portion of human IgG1 by two glycines. The calculated molecular weight of monomeric CHO cell-derived Recombinant Human PD-1 Fc is 55.3 kDa, however, due to glycosylation, it migrates at an apparent molecular weight of approximately 180-200 kDa by SDS-PAGE analysis under non-reducing conditions.

Supplier: PeproTech, Inc.

Description: VAP-1 is a type II membrane cell adhesion protein belonging to the copper/topaquinone oxidase family. It is primarily expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. VAP-1 can catalyze the oxidative deamination of low molecular weight amines, and plays an important role in the migration of lymphocytes to inflamed tissue. Inhibition of VAP-1 can protect against inflammation-related damage to certain injured tissues. Additionally, VAP-1 can function as a significant prognostic marker for certain cancers and cardiovascular diseases. Recombinant Human VAP-1 is a mixture of monomeric and disulfide-linked homodimeric forms of a 737 amino acid polypeptide, corresponding to amino acids 27 to 763 of the VAP-1 precursor. The calculated molecular weight of Recombinant Human VAP-1 is 81.8 kDa.

Supplier: PeproTech, Inc.

Description: 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 Human CNTF is synthesized as a 199 amino acid polypeptide (22.8 kDa) lacking a hydrophobic N-terminal signal for secretion.

Supplier: PeproTech, Inc.

Description: 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.

Supplier: PeproTech, Inc.

Description: TRAIL/Apo2L is a cytotoxic protein, which activates rapid apoptosis in tumor cells, but not in normal cells. TRAIL-induced apoptosis is achieved through binding to two death-signaling receptors, DR4 and DR5. These receptors belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which activates the cell's apoptotic machinery. The full length human TRAIL/Apo2L is a 281 amino acid protein, consisting of a 17 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 243 amino acid extracellular domain. Recombinant Human sTRAIL/Apo2L is a 168 amino acid polypeptide (19.6 kDa), consisting of the TNF-homologous portion of the extracellular domain of the full length TRAIL/Apo2L protein.

Supplier: PeproTech, Inc.

Description: Fractalkine is a CX3CL chemokine that signals through the CX3CR1 receptor. Fractalkine has been shown to chemoattract monocytes, microglia cells and NK cells. Fractalkine is, at this time, the only CXC3C chemokine that contains three amino acid residues between the first and second cysteine residues of the chemokine domain. The Fractalkine gene encodes for a 397 amino acid precursor protein containing a 24 amino acid signal sequence, a chemokine domain, and a "mucin-like stalk" sequence, which is followed by the transmembrane domain containing approximately 20 amino acids, and a C-terminal cytoplasmic domain. The extracellular chemokine domain contains 76 amino acid residues, including the four conserved cysteine residues found in other chemokines. Recombinant Human Fractalkine (CX3CL1) is an 8.5 kDa protein containing 76 amino acid residues, including the four conserved cysteine residues present in CC chemokines.

Supplier: PeproTech, Inc.

Description: Sclerostin, a glycoprotein predominantly secreted by osteocytes, is a member of the Cerberus/DAN family of putative BMP antagonists that functions as an endogenous regulator of the canonical Wnt signaling pathway and an inhibitory regulator of bone homeostasis. Although expressed nearly exclusively by osteocytes, sclerostin can also be found at significant levels elsewhere, such as bone, bone marrow, cartilage, the kidney, and the liver, and has also been shown to be produced by hypertrophic chondrocytes and cementocytes. Like DKK family members DKK-1 and DKK-4, sclerostin plays an important regulatory role in the Wnt/beta-catenin signaling pathway by forming inhibitory complexes with LDL Receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/beta-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/beta-catenin signaling cascade. Sclerostin has also been shown to interact directly with LRP4 via its extracellular domain to facilitate inhibition of Wnt signaling, and can catabolically promote osteoclast activity by increasing osteocyte expression of RANKL. Sclerostin's critical involvement in the regulation of bone formation and resorption is emphasized by two bone dysplasia disorders, sclerosteosis and van Buchem disease (VBD), caused by rare autosomal recessive mutations that result in progressive bone overgrowth and hypermineralization due to markedly decreased sclerostin levels. PeproTech's CHO cell-derived Recombinant Human Sclerostin is a 190-amino-acid-length glycoprotein with a calculated molecular weight of 21.5 kDa. As a result of glycosylation, Recombinant Human Sclerostin migrates with an apparent molecular mass of approximately 28-35 kDa by SDS-PAGE gel, under non-reducing conditions.