Catalog Peptides & Services peptide shop & custom peptide synthesis - p&eShop

Welcome to our Peptide Shop

Discover a wide range of high quality peptides, available for immediate delivery.
Our peptides are meticulously produced, ensuring reliability in your studies
and designed to promote remarkable results in your immune research.

Let's push the boundaries of knowledge and understanding together!

NEUROSCIENCE > INFECTIOUS DISEASE > CANCER >

You can sort the listed peptides according to name, lowest price and release date, for example.

[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)

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)

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)

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)

bioactive peptide

From €60.40*

Details

[beta]-Amyloid (1-11)

Anionic interaction of Aï¿½(1-11) with Factor XII is suspected to cause the massive activation of the C4 (Complement 4) system in cerebrospinal fluid of Alzheimerï¿½s disease patients.

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- 40)

Post-mortem Alzheimer’s diseased brain specimens reveals significant levels of Aß (11-40/42) within insoluble amyloid pools. The ß-secretase enzyme or ß-amyloid precursor protein-cleaving enzyme (BACE) generates the N terminus of Aß, ultimately leading to the production of full-length Aß (1-40/42) or truncated Aß (11-40/42). The abundance of Aß (11-40/42) produced by BACE suggests that their roles in AD pathogenesis may be important.

From €241.50*

Details

[beta]-Amyloid (11-22)

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. Aï¿½ (12ï¿½28) residues are the binding site for apolipoprotein E (apoE) on Aï¿½. This sequence encompasses a hydrophobic domain (residues 14ï¿½21) and a ï¿½-turn (residues 22ï¿½28) which place two hydrophobic domains of Aï¿½ 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aï¿½ peptides into fibrils. The secondary structure of Aï¿½ (12- 28), a neutral peptide, is dominated by a-helix and random coil. The interaction of apoE with residues 12 to 28 of Aï¿½ is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aï¿½ pathology in Alzheimerï¿½s disease (AD). Aï¿½ (11-28) and five other fragments enhanced aggregation of full length Aï¿½ (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 Aï¿½.

From €84.55*

Details