Tripeptide Library Matrix (8000 peptide)
Tripeptide Library Matrix (8000 peptide)
Showing 273–281 of 281 results
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WT-1 Peptide (RMFPNAPYL)
Antigen Peptide WT-1 H-2 Db HLA-A*0201 HLA-B*2705 (RMFPNAPYL) – AA 126-134 for stimulation of antigen-specific T cells in T cell assays such as ELISPOT, ICS, cytotoxity or proliferation assays.
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α-Factor Mating Pheromone, yeast
The alpha factor pheromone arrests yeast in the G1 phase of their cell cycle. Alpha Factor Mating Pheromone induces the expression of mating genes, changes in nuclear architecture, and polarzes growth toward the mating partner. STE2 encodes the alpha factor pheromone receptor (a GPCR) found on mating-type-A cells in yeast.
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β-Amyloid (1-40)
Beta-amyloid peptide (beta-APP) is a 40-residue peptide implicated in the pathogenesis of Alzheimer’s disease (AD) and aged Down’s Syndrome, which is promoted by the acquisition of an additional copy of chromosome 21. The peptide is a proteolytic product of the much larger amyloid precursor protein (APP) encoded by a gene on chromosome 21. The peptide comprises a large extracellular N-terminal domain and a short hydrophobic membrane-spanning domain, followed by a short C-terminal region. Beta-APP both precedes and forms part of the transmembrane region.
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β-Amyloid (1-42), human
This peptide is well suited to the quantitative determination of A 42 peptide. Alzheimer’s disease (AD) is characterized by the presence of extracellular plaques and intracellular neurofibrillary tangles (NFTs) in the brain. The major protein component of these plaques is beta amyloid peptide (A), a 40- to 43- amino-acid peptide cleaved from amyloid precursor protein by secretase (BACE) and a putative (gamma) secretase. Increased release of the ‘longer forms’ of A peptide, A 42 and A 43, which have a greater tendency to aggregate than A 40, occurs in individuals expressing certain genetic mutations, expressing certain ApoE alleles or may other, still undiscovered factors.
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β-Amyloid (1-42), human
This peptide is well suited to the quantitative determination of A 42 peptide. Alzheimer’s disease (AD) is characterized by the presence of extracellular plaques and intracellular neurofibrillary tangles (NFTs) in the brain. The major protein component of these plaques is beta amyloid peptide (A), a 40- to 43- amino-acid peptide cleaved from amyloid precursor protein by secretase (BACE) and a putative (gamma) secretase. Increased release of the ‘longer forms’ of A peptide, A 42 and A 43, which have a greater tendency to aggregate than A 40, occurs in individuals expressing certain genetic mutations, expressing certain ApoE alleles or may other, still undiscovered factors.
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β-Amyloid (25-35)
Beta-amyloid protein (Abeta), a major component of senile plaques of Alzheimer’s disease (AD) in the brain, causes elevation of the intracellular free Ca2+ level and the production of robust free radicals. Beta-amyloid 25-35 induced apoptosis, characterized by decreased cell viability, neuronal DNA condensation, and fragmentation, is associated with an increase in intracellular free Ca2+ level, the accumulation of reactive oxygen species (ROS), and the activation of caspase-3. All of these effects induced by beta-amyloid 25-35 are reversed by genistein.
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β-Endorphin, human
Potent endogenous opioid protein b-Endorphin is derived from propiomelanocortin, b-Endorphin is a protein found in the brain, anterior pituitary, skin, immune system, and other peripheral sites. β-Endorphin is released in response to painful stimuli and b-Endorphin has potent antinociceptive activity mediated through its action on μ receptors in brain and by μ and κ receptors in the spinal cord.