You Searched For: Pendotech

Catalog Number: (76303-590)

Supplier: PeproTech, Inc.

Description: The three mammalian isoforms of TGF-beta, TGF-beta1, beta2, and beta3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of the biologically active TGF-beta isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. The physiological role of TGF-beta3 is still unknown, but its expression pattern suggests a role in the regulation of certain development processes. Recombinant Human TGF-beta3 is a 25.0 kDa protein composed of two identical 112 amino acid polypeptide chains linked by a single disulfide bond.

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Supplier: PeproTech, Inc.

Description: Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Furin is a calcium-dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa-(K/R)-R, where Xaa can be any amino acid. Recombinant Human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor, plus a C-terminal His-tag.

Supplier: PeproTech, Inc.

Description: 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. BD-4 is expressed in the testes, stomach, uterus, neutrophils, thyroid, lungs and kidneys. In addition to its direct antimicrobial activities, BD-4 is chemoattractant towards human blood monocytes. Recombinant Human BD-4 is a 6.0 kDa protein containing 50 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 naïve 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. Recombinant Rat sRANK Ligand is a 19.4 kDa polypeptide comprising the TNF homologous region of RANKL (174 amino acid residues).

Catalog Number: (10781-870)

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.

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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 Rat MIP-1α (CCL3) is a 7.8 kDa protein containing 69 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.

Supplier: PeproTech, Inc.

Description: ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solubilization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in the liver and brain, and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease. Recombinant Human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.

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. Human HGF is expressed as a linear, polypeptide-precursor glycoprotein containing 697 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 234 amino acid residues. Recombinant Human HGF is an 80.0 kDa polypeptide consisting of 697 amino acid residues.

Catalog Number: (76303-722)

Supplier: PeproTech, Inc.

Description: Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-beta 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: 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 Murine sCD40 Ligand is a soluble 16.4 kDa protein containing 149 amino acid residues comprising the receptor binding TNF-like domain of CD40L.

Supplier: PeproTech, Inc.

Description: Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

Supplier: PeproTech, Inc.

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.

Certificates

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: 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.

Certificates

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: 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.