关于 "Cytoskeleton & Motor Proteins" 的结果115+ 个结果

This cyclized peptide which is homologous to the heparin-binding domain of APP, binds strongly to heparin and inhibits binding of ¹²?I-labeled APP to heparin (IC??= 10??M). The peptide blocks the heparan sulfate proteoglycan-dependent stimulatory effect of APP on neurite outgrowth.

Fluorescent dye-labeled Aβ40, excitation at 649 nm, emission at 664 nm. Tide Fluor™ 5WS shows strong fluorescence and excellent photostability.

Fluorescent dye-labeled Aβ40, excitation at 749nm, emission at 775nm. Tide Fluor™ 7WS shows strong fluorescence and excellent photostability.

SEVNLDAEF corresponds to the mutant junctional sequence of the amyloid precursor protein (APP) found in a Swedish family with early-onset Alzheimer's disease, therefore referred to as the 'Swedish' mutation (K670N/M671L). The peptide has been used for assaying cleavage at leucine-aspartate by cathepsin G and chymotrypsin, whereas neither cathepsin B, D nor L generated any products.

This peptide substrate corresponds to the 'Swedish' Lys-Met/Asn-Leu (K670N/M671L) mutation of the amyloid precursor protein (APP) β-secretase cleavage site. It has been used for assaying β-secretase activity.

Amyloid β-protein (1-40) that is N-terminally modified with the fluorescent dye (7-diethylaminocoumarin-3-yl)carbonyl (DAC or DEAC). This derivative can be utilized to assess the binding properties of amyloid β-protein (1-40) for various membranes since it behaves very similar to the native peptide. In aqueous environments the fluorophore is almost non-fluorescent whereas binding to membranes results in an increase in fluorescence intensity (Λex = 430 nm, Λem = 470 nm). Increases in the GM1 ganglioside and cholesterol content in the lipid bilayers facilitated the binding of this peptide. For phosphatidylcholine and phosphatidylserine no affinity was observed.

Amyloid precursor protein (APP) β-secretase from human brain cleaves full-length APP at the amino terminus of the amyloid β-protein (Aβ) sequence, thus leading to the generation and extracellular release of β-cleaved soluble APP and a corresponding cell-associated carboxy-terminal fragment. The subsequent cleavage of the C-terminal fragment by γ-secretase(s) leads to the formation of Aβ. This new peptide represents a potent substrate analog inhibitor of APP β-secretase with IC?? = 30 nM.

Intramolecularly quenched fluorescent substrate containing the ortho-aminobenzoyl (Abz) / N-(2,4-dinitrophenyl)ethylenediamine (EDDnp) groups as the donor / acceptor pair. It corresponds to the Swedish-mutated (JMV2236) β-amyloid precursor protein (βAPP) sequence targeted by β-secretase BACE (β-site APP-cleaving activity). This FRET substrate is more selectively cleaved by BACE1 and BACE2 than by cathepsin D, a disintegrin and metalloprotease 10 (ADAM10), tumor necrosis α-converting enzyme (TACE), presenilin-1 (PS1), or presenilin-2 (PS2).

A 15-residue cyclized APP fragment

Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site of the Swedish mutation of APP, SEVNLDAEF.

CGHGNKSGLMVGGVV.

Membrane-permeable inhibitor of Aβ (1-40) fibrillogenesis.

This fluorescent (FRET) peptide substrate contains the wild-type amyloid precursor protein (APP) β-secretase cleavage site. Mca-SEVKMDAEFRK(Dnp)RR- amide has been used for assaying β-secretase-like activity of thimet oligopeptidase (TOP, EC 3.4.24.15). The results suggested that TOP is a potential β-secretase candidate and is involved in the processing of APP in vivo. See also L-1905.

Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site EVNLDAEF of the Swedish mutation of APP. The kinetic parameters at pH 4.5 are Km = 5.4 µM and kcat = 0.24 min?¹.

A sensitive fluorogenic (FRET) substrate developed for the analysis of γ-secretase from post mortem non-Alzheimer's and Alzheimer's disease human brain isolates.

Intramolecularly quenched fluorescent, presenilin-dependent substrate for assaying γ-secretase activity. The FRET substrate has been used for partial purification and characterization of γ-secretase from post-mortem human brain.

β-amyloid (12-28) TFA 是 β-淀粉样蛋白 (β1-42) 的肽片段。 β1-42 是 42 个氨基酸的蛋白质，是老年斑核心的主要成分。β-amyloid (12-28) 具有聚集特性。β-amyloid (12-28) 有潜力用于阿尔茨海默氏病的研究。