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Supplier: PeproTech, Inc.
Description: Both MIP-1α and MIP-1β are structurally and functionally related CC chemokines. They participate in host response to invading bacterial, viral, parasite and fungal pathogens, by regulating the trafficking, and activation state, of selected subgroups of inflammatory cells (e.g. macrophages, lymphocytes and NK cells). While both MIP-1α and MIP-1β exert similar effects on monocytes, their effect on lymphocytes differ; with MIP-1α selectively attracting CD8+ lymphocytes, and MIP-1β selectively attracting CD4+ lymphocytes. Additionally, MIP-1α and MIP-1β have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1α and MIP-1β are active on human and murine hematopoietic cells. Recombinant Human MIP-1α is a 7.8 kDa protein containing 70 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines. Manufactured using all Animal-Free reagents.

Supplier: PeproTech, Inc.
Description: 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 human 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 Human GDNF is 30.4 kDa.

Supplier: PeproTech, Inc.
Description: Members of the Hedgehog (Hh) family are highly conserved proteins that are widely represented throughout the animal kingdom. The three known mammalian Hh proteins, Sonic (Shh), Desert (Dhh) and Indian (Ihh), are structurally related, and share a high degree of amino acid sequence identity (e.g. Shh and Ihh are 93% identical). The biologically active form of each Hh molecule is obtained by autocatalytic cleavage of their precursor proteins, and each corresponds to approximately one half of the N-terminal portion of the precursor molecule. Although Hh proteins have unique expression patterns and distinct biological roles within their respective regions of secretion, they use the same signaling pathway and can be substituted for one another in experimental systems. Recombinant Murine Sonic Hedgehog (Shh) is a 20.0 kDa protein consisting of 176 amino acid residues, including an N-terminal Ile-Val-Ile sequence substituted for the naturally occurring, chemically modified Cys residue.

Supplier: PeproTech, Inc.
Description: Both MIP-1α and MIP-1β are structurally and functionally related CC chemokines. They participate in host response to invading bacterial, viral, parasite and fungal pathogens, by regulating the trafficking, and activation state, of selected subgroups of inflammatory cells (e.g. macrophages, lymphocytes and NK cells). While both MIP-1α and MIP-1β exert similar effects on monocytes, their effect on lymphocytes differ; with MIP-1α selectively attracting CD8+ lymphocytes, and MIP-1β selectively attracting CD4+ lymphocytes. Additionally, MIP-1α and MIP-1β have also been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. Both human and murine MIP-1α and MIP-1β are active on human and murine hematopoietic cells. Recombinant Human MIP-1β (CCL4) is a 7.6 kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

Supplier: PeproTech, Inc.
Description: TWEAK belongs to the TNF family of ligands, and signals through TWEAKR, also known as TNFRSF12A. TWEAK is expressed in a variety of tissues, including the adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK has the ability to induce NF-κB activation and chemokine secretion, and to exert an apoptotic activity in certain cells, such as HT-29 human adenocarcinoma cells when cultured in the presence of IFN-γ. TWEAK also promotes proliferation and migration of endothelial cells. The human TWEAK gene encodes for a 249 amino acid type II transmembrane protein, which contains a 21 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 207 amino acid extracellular domain. Recombinant Human TWEAK is a soluble 17.0 kDa polypeptide (154 amino acid residues) comprising the TNF-homologous region of TWEAK, and is generated by proteolytic processing of the full length membrane-anchored TWEAK protein.Manufactured using all Animal-Free reagents.

Supplier: PeproTech, Inc.
Description: p16-INK4a is a nuclear protein that regulates the cell cycle by inhibiting cyclin-dependent kinase-4 (CDK4) and CDK6. p16-INK4a inhibits CDK activity by binding to the CDK molecules in a manner that interferes with their ability to interact with cyclin D. This activity has the effect of suppressing tumor formation and growth, and of inducing replicative senescence in various normal cells, including stem cells. The expression of p16-INK4a steadily increases with age, and tends to accumulate in stem cell compartments. The deletion, rearrangement, or mutation of the p16-INK4a gene is frequently found in melanomas, as well as in certain other types of cancer. p16-INK4a and other transcription factors have been introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors and other nuclear proteins into primary, as well as transformed, cells. Recombinant Human p16-INK4a-TAT expressed in

Supplier: PeproTech, Inc.
Description: 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 a 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-BB is a 24.4 kDa disulfide-linked homodimer of two β chains (218 total amino acids).

Supplier: PeproTech, Inc.
Description: 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 Rat Resistin is a 20.0 kDa, disulfide-linked, homodimeric protein composed of two 94 identical amino acid chains linked by a single disulfide bond.

Catalog Number: (76303-888)
Supplier: PeproTech, Inc.
Description: 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 GFRalpha (alpha1-alpha4) 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, Inc.
Description: 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.

Supplier: PeproTech, Inc.
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.
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: 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 GFRalpha (alpha1-alpha4) 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, Inc.
Description: 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.

Supplier: PeproTech, Inc.
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.
Catalog Number: (76303-648)
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. Recombinant Human sRANK Ligand is a 20.0 kDa polypeptide comprising the TNF-homologous region of RANKL (176 amino acid residues).


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