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1594 results for "Peprotech"

"Peprotech"

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Rat Recombinant PlGF-1 (from E. coli)

Supplier: Peprotech

PlGF-1 is an angiogenic factor that belongs to the cysteine-knot superfamily of growth factors. PlGF-1 is expressed in placental tissues, the colon, and mammary carcinomas. It signals through the VEGFR-1/FLT1 receptor, and stimulates endothelial cell proliferation and migration. Recombinant Rat PlGF-1 is a 30.3 kDa disulfide-linked homodimeric protein of two 135 amino acid polypeptide chains.

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Human Recombinant TIMP-1 (from E. coli)

Supplier: Peprotech

TIMP-1 is an extracellular inhibitor of MMPs, including MMP-1, -2, -3, -7, -8, -9, -10, -11, -12, -13, and -16. It belongs to the I35 (TIMP) family of irreversible protease inhibitors that function as key modulators of extracellular matrix degradation during tissue development and remodeling. TIMP-1 can also act through an MMP-independent mechanism to promote erythropoiesis by stimulating proliferation and differentiation of erythroid progenitors. Recombinant Human TIMP-1 is a 20.6 kDa protein containing 184 amino acid residues.

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Human Recombinant TIMP-2 (from E. coli)

Supplier: Peprotech

TIMP-2 is an extracellular inhibitor of MMPs, including MMP-1, -2, -3, -7, -8, -9, -10, -12, -13, -14, -15, -16 and -19. It belongs to the I35 (TIMP) family of irreversible protease inhibitors that function as key modulators of extracellular matrix degradation during tissue development and remodeling. TIMP-2 can also act through a MMP-independent mechanism inhibiting endothelial cell proliferation in vitro and demonstrates anti-angiogenic activities Recombinant Human TIMP-2 is a 21.8 kDa protein containing 194 amino acid residues.

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Human Recombinant MMP-1 (from E. coli)

Supplier: Peprotech

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.

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Human Recombinant MMP-2 (from E. coli)

Supplier: Peprotech

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-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant Human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).

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Human Recombinant MMP-3 (from E. coli)

Supplier: Peprotech

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-3 degrades fibronectin, laminin, collagens III, IV, and X, and cartilage proteoglycans. Recombinant Human MMP-3 is a 42.8 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids).

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Human Recombinant beta-NGF (from E. coli)

Supplier: Peprotech

β-NGF is a neurotrophic factor structurally related to BDNF, NT-3 and NT-4. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. β-NGF is a potent neurotrophic factor that signals through its receptor β-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. β-NGF also acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. The functional form of Recombinant Human β-NGF is a non-covalently-linked homodimer of two 13.5 kDa, polypeptide monomers that each contain 120 amino acids and three disulfide bonds, which are required for biological activity.

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Human;Mouse;Rat Recombinant BDNF (from E. coli)

Supplier: Peprotech

BDNF is a member of the NGF family of neurotrophic growth factors. Like other members of this family, BDNF supports neuron proliferation and survival. BDNF can bind to a low affinity cell surface receptor called LNGFR, which also binds other neurotrophins such as NGF, NT-3 and NT-4. However, BDNF mediates its neurotrophic properties by signaling through a high affinity cell surface receptor called gp145/trkB. BDNF is expressed as the C-terminal portion of a 247 amino acid polypeptide precursor, which also contains a signal sequence of 18 amino acid residues and a propeptide of 110 amino acid residues. Recombinant Human/Murine/Rat BDNF is a 27.0 kDa homodimer of two 120 amino acid subunits linked by strong non-covalent interactions.

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Human Recombinant NT-3 (from E. coli)

Supplier: Peprotech

NT-3 is a neurotrophic factor structurally related to β-NGF, BDNF, and NT-4. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. NT-3 is expressed by neurons of the central nervous systems, and can signal through the trk receptors. NT-3 promotes the growth and survival of nerve and glial cells. The amino acid sequences of human, murine and rat NT-3 are identical. Recombinant Human NT-3 is a noncovalently linked homodimer of two 13.6 kDa polypeptide monomers (240 total amino acid residues).

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Human Recombinant NT-4 (from E. coli)

Supplier: Peprotech

NT-4 is a neurotrophic factor structurally related to β-NGF, BDNF, and NT-3. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. NT-4 is expressed in the prostate, thymus, placenta, and skeletal muscle. NT-4 can signal through the LNGFR and trkB receptors, and promotes the survival of peripheral sensory sympathetic neurons. Recombinant Human NT-4 is a noncovalently linked homodimer of two 14.0 kDa polypeptide monomers (260 total amino acid residues).

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Human Recombinant CDNF (from E. coli)

Supplier: Peprotech

CDNF is a secreted neurotrophic factor that is expressed in brain, neuronal and certain non-neuronal tissues. It has been shown to promote survival, growth and function of dopamine-specific neurons. CDNF and its structural homolog, MANF, each contain an N-terminal saposin-like lipid binding domain, and a carboxyl-terminal domain, which is not homologous to previously characterized protein structures. CDNF and MANF can prevent 6-OHDA-induced degeneration of dopaminergic neurons by triggering survival pathways in a rat experimental model of Parkinson’s disease. Recombinant Human CDNF is an 18.5 kDa protein consisting of 162 amino acids, including 8 cysteine residues.

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Human Recombinant MANF (from E. coli)

Supplier: Peprotech

MANF is a secreted neurotrophic factor that is expressed in brain, neuronal and certain non-neuronal tissues. It has been shown to promote the survival, growth and function of dopamine-specific neurons. MANF and its structural homolog CDNF each contain an N-terminal, saposin-like, lipid-binding domain, and a carboxyl-terminal domain that is not homologous to previously characterized protein structures. MANF and CDNF can prevent 6-OHDA-induced degeneration of dopaminergic neurons by triggering survival pathways in a rat experimental model of Parkinson's disease. Recombinant Human MANF is an 18.1 kDa protein consisting of 158 amino acids, including 8 cysteine residues.

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Human Recombinant GDNF (from E. coli)

Supplier: Peprotech

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.

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Human Recombinant Neurturin (from E. coli)

Supplier: Peprotech

Neurturin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, artemin, and persephin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Neurturin signals through a multicomponent receptor system, composed of RET and one of four GFRα (α1-α4) receptors. Neurturin promotes the development and survival of sympathetic and sensory neurons by signaling through a receptor system composed of RET and GFRα2. The functional form of human neurturin is a disulfide-linked homodimer, of two 11.8 kDa polypeptide monomers (204 total amino acid residues). Each monomer contains seven conserved cysteine residues, one of which (Cys 69) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.

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Human Recombinant Persephin* (from E. coli)

Supplier: Peprotech

Persephin is a disulfide-linked, homodimeric, neurotrophic factor structurally related to GDNF, artemin, and neurturin. These proteins belong to the cysteine knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFR α (α1-α4) receptors. The GFRα4 was first identified in chicken, and was later shown to be the preferential binding subunit for persephin. Persephin promotes the survival of ventral midbrain dopaminergic neurons and motor neurons after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud branching. However, in contrast to GDNF and neurturin, persephin does not support the survival of peripheral neurons. Recombinant Human Persephin is a disulfide-linked homodimer, composed of two 10.4 kDa polypeptide chains (194 total amino acid residues). Each chain contains seven conserved cysteine residues, one of which (Cys 64) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.

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Human Recombinant CNTF (from E. coli)

Supplier: Peprotech

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.

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