usps-logo.jpg?1721728722
Ultrafast Ultrasonic Synthesis
Catalog peptides: immediate delivery
ISO 9001/2015 certified
1000 peptides & peptide pools
30 years of experience in peptide synthesis
Go to homepage
€0.00*

Type in Search Term here to find products and any content
or filter the current selection by criteria below:

Filter
Filter and select current selecztion:

Catalog Peptides - p&eShop

Ready off the shelf peptides - fast delivery

High quality 95% purity catalog peptides for

cancer cell signaling
neuroscience peptide & protein analysis
infectious diseases  hormones
[Ala8] - Humanin, [Ala8] - HN, Shna
Protection activity of humanin (HN) against neuronal cell death is abrogated in this peptide, where Cys8 is substituted by Ala.

From €96.60*
Details
[alpha]-Bag Cell Peptide (1 - 7) ( APRLRFY )
The heptapeptide APRLRFY from Aplysia parvula acts as a neurotransmitter locally, upon neurons of the abdominal ganglion and as a hormone by diffusing into the circulating hemolymph and modulating the activity of other organs. It specifically causes contraction of smooth muscle in the ovotestis and expulsion of the egg string.

From €54.35*
Details
[alpha]-Bag Cell Peptide (1 - 8) ( APRLRFYS )
The octapeptide APRLRFYS from Aplysia parvula acts as a neurotransmitter locally, upon neurons of the abdominal ganglion and as a hormone by diffusing into the circulating hemolymph and modulating the activity of other organs. It specifically causes contraction of smooth muscle in the ovotestis and expulsion of the egg string.

From €54.35*
Details
[alpha]-Bag Cell Peptide (1 - 9) ( APRLRFYSL )
The nonapeptide APRLRFYSL from Aplysia parvula acts as a neurotransmitter locally, upon neurons of the abdominal ganglion and as a hormone by diffusing into the circulating hemolymph and modulating the activity of other organs. It specifically causes contraction of smooth muscle in the ovotestis and expulsion of the egg string.

From €54.35*
Details
[alpha]-Casein (90-95) ( RYLGYL )
bioactive peptide

From €60.40*
Details
beta-Amyloid (1-11) ( DAEFRHDSGYE )
The beta-Amyloid 1-11 peptide with the amino acid sequence DAEFRHDSGYE is a linear peptidic epitope (epitope ID 104443) studied as part of several isoforms of Amyloid-beta precursor protein (APP) from Homo sapiens: Isoform APP751 (UniProt:P05067-8)  Isoform L-APP752 (UniProt:P05067-9)  Isoform L-APP696 (UniProt:P05067-5) and  Isoform L-APP677 (UniProt:P05067-3). Anionic interaction of Aß 1-11 with Factor XII is suspected to cause the massive activation of the C4 (Complement 4) system in cerebrospinal fluid of Alzheimer's disease patients.  DAEFRHDSGYE has been studied for immune reactivity and has been tested in T cell assays and B cell assays.

From €84.55*
Details
[beta]-Amyloid (1-14)
Beta-amyloid peptide (Abeta), the major constituent of amyloid plaques in the brains of Alzheimer’s patients, is thought to be the cause of Alzheimer’s Disease (AD). AD is the most common neurodegenerative disease and afflicts about 10% of the population over 60.

From €84.55*
Details
[beta]-Amyloid (1-15)
Aβ (1-15) was used in a study investigating the presence of conformational epitope/s (mimotope/s) on fibrillar amyloid β-protein (1-42). The N-terminal Aβ fragments Aβ1-14, Aβ1-15, and Aβ1-16 are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The fragments can serve as biomarkers in clinical studies of the effect of such inhibitors.

From €84.55*
Details
[beta]-Amyloid (1-16)
The Cu²⁺ complex of this soluble amyloid β-protein fragment showed significant oxidative activities toward the catechol-like substrate 1,2,3-trihydroxylbenzene (pyrogallol) and plasmid DNA cleavage. The N-terminal Aβ fragments Aβ1-14, Aβ1-15, and Aβ1-16 are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The fragments can serve as biomarkers in clinical studies of the effect of such inhibitors. Proteins interactions with reactive oxygen agents may result in covalent modifications of amino acid residues in proteins, formation of protein-protein cross-linkages and oxidation of the protein backbone resulting in protein fragmentation. Oxidation targets for Aß(1-16) are the histidine residues coordinated to the metal ions. Copper is bound to Aß in senile plaque of Alzheimer’s disease with Aß (1-16) taking part in the coordination of the Cu2+ ions. Cu2+ and Zn2+ are linked with the neurotoxicity of Aß and free radical damage.

From €84.55*
Details
[beta]-Amyloid (1-28)
The three-dimensional solution structure of Aß (1-28) reveals the folding of the peptide to form a predominantly a-helical structure with a bend centered at residue 12 and the side chains of histidine-13 and lysine-16 in close proximity, residing on the same face of the helix. Their proximity may constitute a binding motif with the heparan sulfate proteoglycans. Aß (1-28) is highly hydrophilic and shares sequences with bA4, the major component of Aß. Its assembly is fibrillar, i.e., elongated in a single direction. Reports show that synthetic peptides Aß (1-40) and Aß (1-28) have significant effects on normal human plasma cholesterol esterification rate. Both peptides (at concentration of 1 ng/mL) inhibit plasma cholesterol esterification rate by 40-50% compared to the control value.

From €181.15*
Details
[beta]-Amyloid (1-39)
A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-39) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).

From €362.25*
Details
[beta]-Amyloid (1-40)
A number of Aß protein variants, differing only at their carboxy terminus (1-39, 1-40, 1-42 and 1-43), are identified as the major components of the cerebral amyloid deposits in Alzheimer’s disease. The length of the C-terminus is a critical determinant of the rate of amyloid formation (“kinetic solubility”), with only a minor effect on the thermodynamic solubility. Amyloid formation by the kinetically soluble peptides (e.g. 1-40) can be nucleated, or “seeded” by peptides which include the critical C-terminal residues (1-42, 26-42, 26-43, 34-42).

From €362.25*
Details
[beta]-Amyloid (10-35)
Amyloid β-protein (10-35), YEVHHQKLVFFAEDVGSNKGAIIGLM, was used as a truncated peptide model for the full-length amyloid β-proteins (1-40) and (1-42) in high-resolution structural studies. In contrast to the full-length amyloid β-proteins, amyloid β-protein (10-35) allowed the controlled and reproducible formation of homogeneous fibrils from aqueous solutions of defined pH, ionic strength and soluble peptide concentration necessary for high-resolution structural studies.

From €144.90*
Details
beta-Amyloid (11-22)
Beta-amyloid peptide (Abeta), the major constituent of amyloid plaques in the brains of Alzheimer’s patients, is thought to be the cause of Alzheimer’s Disease (AD). AD is the most common neurodegenerative disease and afflicts about 10% of the population over 60.

From €84.55*
Details
[beta]-Amyloid (12-28)
Injection of the amyloid ?-protein fragment VHHQKLVFFAEDVGSNK into different limbic system structures in mice impaired retention with remarkably similar efficacy and in a dose-dependent manner. A? (12-28) and other A? fragments may exert dysregulatory cognitive effects by incoordination of K? channel function in neurons, glia and endothelial cells. A� (12�28) residues are the binding site for apolipoprotein E (apoE) on A�. This sequence encompasses a hydrophobic domain (residues 14�21) and a �-turn (residues 22�28) which place two hydrophobic domains of A� 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of A� peptides into fibrils. The secondary structure of A� (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of A� is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of A� pathology in Alzheimer�s disease (AD). A� (11-28) and five other fragments enhanced aggregation of full length A� (1-40). All of the peptides that enhance aggregation contained either residues 17 to 20 or 30 to 35, indicating the importance of these regions for promoting aggregation of full-length A�.

From €84.55*
Details
[beta]-Amyloid (13-27)
This β-Amyloid peptide 13 to 27 amino acid residues was used to study the kinetics of β-amyloid formation.

From €84.55*
Details
[beta]-Amyloid (16-23) ( KLVFFAED )
This octapeptide beta-Amyloid 16 to 23 was used in exploring the design of potential inhibitors of amyloidogenesis. This peptide is capable of forming thin flakes, while the shortest fibril-forming sequence was found to be the decapeptide b-Amyloid 14 to 23.

From €60.40*
Details
[beta]-Amyloid (22-35)
Aβ (22-35), EDVGSNKGAIIGLM, forms amyloid fibrils in vitro resembling those of the β-amyloid protein in senile plaques and exhibits a toxicity profile that parallels that of full-length Aβ (1-40) and Aβ (1-42) in hippocampal and cortical neurons in cell culture.

From €84.55*
Details
[beta]-Casomorphin (1-7), bovine ( YPFPGPI )
#