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Merck

A2201

Amyloid β-Protein Fragment 35-25

≥95% (HPLC)

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250 μG

CHF 156.00

1 MG

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Informazioni su questo articolo

Formula empirica (notazione di Hill):
C45H81N13O14S
Numero CAS:
Peso molecolare:
1060.27
NACRES:
NA.32
PubChem Substance ID:
UNSPSC Code:
51111800
MDL number:
Form:
powder
Assay:
≥95% (HPLC)

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InChI key

IDGOADDOQWKZOX-UHFFFAOYSA-N

SMILES string

CCC(C)C(NC(=O)CNC(=O)C(CC(C)C)NC(=O)C(N)CCSC)C(=O)NC(C(C)CC)C(=O)NC(C)C(=O)NCC(=O)NC(CCCCN)C(=O)NC(CC(N)=O)C(=O)NC(CO)C(=O)NCC(O)=O

InChI

1S/C45H81N13O14S/c1-9-24(5)36(57-34(62)20-50-40(67)29(17-23(3)4)54-39(66)27(47)14-16-73-8)45(72)58-37(25(6)10-2)44(71)52-26(7)38(65)49-19-33(61)53-28(13-11-12-15-46)42(69)55-30(18-32(48)60)43(70)56-31(22-59)41(68)51-21-35(63)64/h23-31,36-37,59H,9-22,46-47H2,1-8H3,(H2,48,60)(H,49,65)(H,50,67)(H,51,68)(H,52,71)(H,53,61)(H,54,66)(H,55,69)(H,56,70)(H,57,62)(H,58,72)(H,63,64)

assay

≥95% (HPLC)

form

powder

UniProt accession no.

storage temp.

−20°C

Quality Level

Gene Information

human ... APP(351)

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Questo articolo
A5080A9810A4723
assay

≥95% (HPLC)

assay

≥95% (HPLC)

assay

≥95% (HPLC)

assay

≥90% (HPLC)

form

powder

form

powder

form

powder

form

lyophilized powder

UniProt accession no.

P05067

UniProt accession no.

P05067

UniProt accession no.

P05067

UniProt accession no.

P05067

Gene Information

human ... APP(351)

Gene Information

human ... APP(351)

Gene Information

human ... APP(351)

Gene Information

human ... APP(351)

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

Amyloid β precursor protein (APP) is a type-1 transmembrane protein.[1] APP is expressed widely and mainly found in the synapses and neurons.[2] The APP gene is mapped to human chromosome 21q21.3.[3]

Application

Amyloid β-Protein Fragment 35-25 has been used as a control peptide for Aβ-induced apoptosis to study the role of hepcidin overexpression in astrocytes against amyloid-β induced brain damage in mice.[4]

Biochem/physiol Actions

Proteolytic processing of amyloid β precursor protein (APP) forms the β amyloid protein (Aβ) as part of the brain amyloid plaques[1] which are the key biomarkers in Alzheimer′s disease. APP is known to be associated with neurogenesis, synapse formation, axonal transport, neuronal migration and neurite outgrowth. It is also related to mitochondria-associated endoplasmic reticulum membranes (MAMs) activity, antimicrobial protection, cholesterol, and iron homeostasis.[2][1] Amyloid β-Protein Fragment 35-25 is an inactive control.

Other Notes

The N—C inverted sequence of fragment 25-35

Classe di stoccaggio

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Anatoliy I Yashin et al.
Mechanisms of ageing and development, 196, 111477-111477 (2021-04-03)
Emerging evidence from experimental and clinical research suggests that stress-related genes may play key roles in AD development. The fact that genome-wide association studies were not able to detect a contribution of such genes to AD indicates the possibility that
Jasmine Chebli et al.
Scientific reports, 11(1), 19115-19115 (2021-09-29)
Amyloid precursor protein (APP) is expressed in many tissues in human, mice and in zebrafish. In zebrafish, there are two orthologues, Appa and Appb. Interestingly, some cellular processes associated with APP overlap with cilia-mediated functions. Whereas the localization of APP
Elvis Cuevas et al.
Metabolic brain disease, 34(5), 1365-1374 (2019-07-04)
The amyloid β-peptide (Aβ) is transported across the blood-brain barrier (BBB) by binding with the receptor for advanced glycation end products (RAGE). Previously, we demonstrated that the Aβ fraction 25-35 (Aβ25-35) increases RAGE expression in the rat hippocampus, likely contributing
Alzheimer's disease: amyloid beta-peptide antibody vaccine as plaque remover.
A Kumar
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Cell death discovery, 6(1), 113-113 (2020-12-11)
Progressive iron accumulation in the brain and iron-induced oxidative stress are considered to be one of the initial causes of Alzheimer's disease (AD), and modulation of brain iron level shows promise for its treatment. Hepcidin expressed by astrocytes has been

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