You Searched For: Pendotech

Supplier: PeproTech, Inc.

Description: 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.

Supplier: PeproTech, Inc.

Description: As a member of the IL-12 family of heterodimeric cytokines that also includes IL-12, IL-23, and IL-35, IL-27 is formed by the association of an IL-27-p28 subunit (also known as IL-30) with the Epstein-Barr Virus (EBV)-induced Gene 3 (EBI3) subunit (also known as IL-27B). Expressed by antigen-presenting cells (APCs) in the early phases of antigen-mediated activation, IL-27 acts as a critical initiator of adaptive immune responses by promoting the rapid clonal expansion of naïve CD4+ T cells, IFN-γ production, and Th1 polarization. IL-27 elicits its effects through receptor complexes IL-27R (also known as TCCR/WSX-1) and gp130, a receptor shared by IL-6. Mainly expressed in monocytes, endothelial cells, and dendritic cells, IL-27 plays an important role alongside IL-6 in the regulation of inflammation and autoimmunity; directly antagonizing IL-6’s stimulation of CD4+ T cell proliferation and Th17 differentiation. Recombinant Human IL-27 produced from

Supplier: PeproTech, Inc.

Description: The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-I is 7.6 kDa.

Supplier: PeproTech, Inc.

Description: Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-β family, and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-β ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of Noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Human Noggin is a 46 kDa disulfide-linked homodimer consisting of two 205 amino acid polypeptide chains. Monomeric glycosylated noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.

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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 is an 8.5 kDa protein containing 76 amino acid residues, including the four conserved cysteine residues present in CC chemokines. Recombinant Rat Fractalkine (CX3CL1) is an 8.7 kDa protein containing 76 amino acid residues, including the four conserved cysteine residues present in CC chemokines.

Supplier: PeproTech, Inc.

Description: ANG-2 binds to the endothelial cell specific receptor Tie-2, but, in contrast to ANG-1, does not induce tyrosine phosphorylation. Consequently, ANG-2 modulates ANG-1 activation of Tie-2 and, depending on the physiological and biochemical environment, can act either as an agonist or antagonist of Tie-2 induced angiogenesis. The signaling interactions of ANG-1, ANG-2 and Tie-2, along with less characterized ANG-3 and ANG-4, are required for embryonic and adult angiogenesis. Physiologically, ANG-1 and ANG-2 are associated with sprouting, tube formation, and structural integrity of newly formed blood vessels. Mature human ANG-2 is a secreted protein containing 480 amino acid residues. ANG-2 is composed of an alpha-helix-rich “coiled coil” N-terminal domain and fibrinogen-like C-terminal domain. ANG-2 exists predominantly in the form of a disulfide-linked dimer. Recombinant Human ANG-2 is a C-terminal histidine-tagged glycoprotein which migrates with an apparent molecular mass of 60.0 – 70.0 kDa by SDS-PAGE under reducing conditions. Sequencing analysis shows an N-terminal sequence starting with residue 68 (D) of the ANG-2 precursor protein. The calculated molecular weight of Recombinant Human ANG-2 is 50.1 kDa.

Catalog Number: (76304-284)

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.

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Supplier: PeproTech, Inc.

Description: CD30 ligand (CD30L) is a type-II membrane-associated glycoprotein belonging to the TNF superfamily and is expressed primarily on certain B cells, T cells, and monocytes. CD30L binds specifically to CD30 (receptor), which is expressed on activated, but not resting, B and T cells, in lymphomas and various chronically inflamed tissues. CD30L/CD30 interactions initiate a signaling cascade that can ultimately lead to the activation of NF-κB. CD30L/CD30 signaling exerts pleiotropic effects on normal cells, including cell death, differentiation, and cell division. Certain diseases, including Hodgkin’s lymphoma, allergic inflammation, diabetes (in NOD mice), and mycobacterial infection can also be affected by CD30L/CD30 signaling. The CD30L gene encodes for a 234 amino acid type II transmembrane protein, which contains a 37 amino acid cytoplasmic sequence, a 25 amino acid transmembrane domain and a 172 amino acid extracellular domain. Recombinant Human soluble CD30L (sCD30L) is a 188 amino acid polypeptide corresponding to the extracellular domain, and contains an 8 residue N-terminal His-Tag. The calculated molecular weight of Recombinant Human sCD30 Ligand is 21.3 kDa.

Catalog Number: (76303-958)

Supplier: PeproTech, Inc.

Description: HGF is a potent, mesenchymally-derived mitogen for mature parenchymal hepatocytes, and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include the induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Murine HGF is expressed as a linear, polypeptide-precursor glycoprotein containing 696 amino acid residues. Proteolytic processing of this precursor generates the biologically active heterodimeric form of HGF, which consists of two polypeptide chains (alpha-chain and beta-chain) held together by a single disulfide bond resulting in formation of a biologically active heterodimer. The alpha-chain consists of 463 amino acid residues and four kringle domains. The beta-chain consists of 233 amino acid residues. Recombinant Murine HGF is a 79.3 kDa polypeptide consisting of 696 amino acid residues.

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Supplier: PeproTech, Inc.

Description: IL-21 is a pleiotropic cytokine produced by CD4+ T cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL-21 include: inducing the differentiation of T-cell-stimulated B-cells into plasma cells and memory B-cells; the stimulation of IgG production in conjunction with IL-4; and the induction of apoptotic effects in naïve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the γ chain (γc) found in other cytokine receptors, including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events, which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3. Recombinant Human IL-21 is a 15.4 kDa protein consisting of 132 amino acid residues.

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Catalog Number: (76303-726)

Supplier: PeproTech, Inc.

Description: DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head-forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play important regulatory roles 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. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/beta-catenin signaling cascade. It has been suggested that by inhibiting Wnt/beta-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Mature human DKK-1 expressed in HEK293 cells is a 35-40 kDa glycoprotein containing 235 amino acid residues. The calculated molecular weight of Recombinant Human DKK-1 expressed in HEK293 cells is 25.8 kDa.

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Supplier: PeproTech, Inc.

Description: IL-21 is a pleiotropic cytokine produced by CD4+ T cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL-21 include: inducing the differentiation of T-cell-stimulated B-cells into plasma cells and memory B-cells; the stimulation of IgG production in conjunction with IL-4; and the induction of apoptotic effects in naïve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the γ chain (γc) found in other cytokine receptors, including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events, which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3. Recombinant Murine IL-21 is a 15.0 kDa protein consisting of 130 amino acid residues.

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Supplier: PeproTech, Inc.

Description: 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 sCD40 ligand is a 16.3 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L.

Supplier: PeproTech, Inc.

Description: The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-II is 7.5 kDa.

Supplier: PeproTech, Inc.

Description: VEGF-D, a member of the VEGF/PDGF family of structurally related proteins, is a potent angiogenic cytokine. It promotes endothelial cell growth, promotes lymphangiogesis, and can also affect vascular permeability. VEGF-D is highly expressed in the lung, heart, small intestine and fetal lung, and at lower levels in the skeletal muscle, colon, and pancreas. It forms cell surface-associated, non-covalent, disulfide-linked homodimers, and can bind and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4) receptors. During embryogenesis, VEGF-D may play a role in the formation of the venous and lymphatic vascular systems. It also participates in the growth and maintenance of differentiated lymphatic endothelium in adults. Both VEGF-C and VEGF-D are over-expressed in certain cancers, and the resulting elevated levels of VEGF-C or VEGF-D tend to correlate with increased lymphatic metastasis. Recombinant Human VEGF-D is a 26.2 kDa, non-disulfide linked, homodimeric protein consisting of two 117 amino acid polypeptide chains. Due to glycosylation, the protein migrates as a 20.0-22.0 kDa band by SDS-PAGE analysis under non-reducing conditions.

Supplier: PeproTech, Inc.

Description: HGF is a potent, mesenchymally-derived mitogen for mature parenchymal hepatocytes, and acts as a growth factor for a broad spectrum of tissues and cell types. HGF signals through a transmembrane tyrosine kinase receptor known as MET. Activities of HGF include the induction of cell proliferation, motility, morphogenesis, inhibition of cell growth, and enhancement of neuron survival. HGF is a crucial mitogen for liver regeneration processes, especially after partial hepatectomy and other liver injuries. Human and murine HGF are cross-reactive. Murine HGF is expressed as a linear, polypeptide-precursor glycoprotein containing 696 amino acid residues. Proteolytic processing of this precursor generates the biologically active heterodimeric form of HGF, which consists of two polypeptide chains (α-chain and β-chain) held together by a single disulfide bond resulting in formation of a biologically active heterodimer. The α-chain consists of 463 amino acid residues and four kringle domains. The β-chain consists of 233 amino acid residues. Recombinant Murine HGF is a 79.3 kDa polypeptide consisting of 696 amino acid residues.