- Cat.No. 상품명 정보
-
GP10118
Amyloid Beta-Peptide (1-40) (human)
인간 Amyloid β-Peptide (1-40) (C194H295N53O58S1)은 H2N-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA-OH 시퀀스를 가진 펩타이드로, 분자량은 4329.8입니다. 아밀로이드 베타(Aβ 또는 Abeta)는 아밀로이드 전구 단백질에서 처리된 36~43개의 아미노산으로 이루어진 펩타이드입니다.
- GC45382 Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt)
-
GP10082
Amyloid Beta-peptide (25-35) (human)
알츠하이머 아밀로이드 베타 펩타이드의 단편인 인간 Amyloid beta-peptide (25-35)은 신경독성 효과가 있습니다.
- GP10094 Amyloid β-peptide (10-35), amide
- GP10049 Amyloid Beta-Peptide (12-28) (human)
- GP10057 Amyloid β-Peptide (10-20) (human)
- GC43650 FAM-Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt) FAM-Amyloid-β (1-40) peptide is a fluorescently labeled amyloid-β peptide.
- GC42798 Amyloid-β (1-38) Peptide (trifluoroacetate salt) Amyloid-β (1-38) (Aβ38) peptide is a fragment of the Aβ42 peptide.
- GC42803 Amyloid-β (25-35) Peptide (human) (trifluoroacetate salt) Amyloid-β (25-35) (Aβ (25-35)) is an 11-residue fragment of the Aβ protein that retains the physical and biological characteristics of the full length peptide.
- GC46851 Amyloid-β (1-42) Peptide (trifluoroacetate salt) A 42-amino acid protein fragment of amyloid-β
- GC46850 Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt) A neuropeptide with diverse biological activities
- GC42799 Amyloid-β (17-40) Peptide (human) (trifluoroacetate salt) Amyloid-β (Aβ) (17-40) is a 24-residue fragment of the Aβ protein that is formed via post-translational processing of amyloid precursor protein (APP) by α- and γ-secretases.
- GC40127 Amyloid-β (22-35) Peptide (trifluoroacetate salt) Amyloid-β (Aβ) (22-35) is a 13-residue fragment of Aβ that corresponds to residues 693-705 of the human amyloid precursor protein (APP) full-length sequence.
- GC44987 TAMRA-Amyloid-β (1-42) Peptide (trifluoroacetate salt) TAMRA-Amyloid-β (1-42) peptide is a fluorescently labeled peptide.
- GC44986 TAMRA-Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt) TAMRA-Amyloid-β (1-28) peptide is a fluorescently labeled peptide.
- GC42505 5-FAM-Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt) 5-FAM-Amyloid-β (1-28) peptide is a fluorescently labeled peptide.
- GC40160 Biotin-Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt) Biotin-amyloid-β (1-28) peptide is a biotinylated peptide.
- GC40130 5-FAM-Amyloid-β (1-42) Peptide (human) (trifluoroacetate salt) 5-FAM-Amyloid-β (1-42) peptide is a fluorescently labeled amyloid-β peptide.
- GC40128 TAMRA-Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt) TAMRA-Amyloid-β (1-40) peptide is a fluorescently labeled peptide.
- GC42937 Biotin-Amyloid-β (1-42) Peptide (trifluoroacetate salt) Biotin-amyloid-β (1-42) peptide is an affinity probe that allows amyloid-β (1-42) (Aβ42) to be detected or immobilized through interaction with the biotin ligand.
- GC42801 Amyloid-β (1-8) Peptide Amyloid-β (1-8) is a wild-type control for the mutation-containing amyloid-β (1-8, A2V) peptide .
-
GC18339
Amyloid β-Peptide (1-42) human
Amyloid β-Peptide (1-42) human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.
- GC45465 Glp-Amyloid-β (3-40) Peptide (human) (trifluoroacetate salt)
- GC35335 Amyloid β-peptide (1-40) rat 아밀로이드 β-펩티드(1-40) 쥐는 아밀로이드 β의 쥐 형태입니다.
- GC35334 Amyloid β Peptide (42-1)(human) 아밀로이드 β 펩티드(42-1)(인간)는 아밀로이드 β의 비활성 형태입니다. 펩티드(1-42).
- GC42804 Amyloid-β (40-1) Peptide (human) (trifluoroacetate salt) Amyloid-β (40-1) peptide (Aβ (40-1)) is a peptide that contains the reverse sequence of Aβ (1-40) peptide.
- GC42802 Amyloid-β (1-8, A2V) Peptide Amyloid-β (1-8, A2V) is a truncated form of amyloid-β (Aβ) that contains a valine to alanine substitution at position 2 of the Aβ numbering convention (Aβ A2V), which corresponds to position 673 of the amyloid precursor protein (APP) numbering convention (APP A673V).
- GC42800 Amyloid-β (17-42) Peptide (human) (trifluoroacetate salt) Amyloid-β (Aβ) (17-42) is a 26-residue fragment of the Aβ protein that is formed via post-translational processing of amyloid precursor protein (APP) by α- and γ-secretases.
- GC40129 Biotin-Amyloid-β (1-40) Peptide (trifluoroacetate salt) Biotin-amyloid-β (1-40) (biotin-Aβ40) is an affinity probe that allows amyloid-β (1-40) (Aβ40) to be detected or immobilized through interaction with the biotin ligand.
- GC40126 Amyloid-β Precursor Protein (96-110) Peptide (cyclized) (human) (trifluoroacetate salt) Amyloid-β precursor protein (96-110) peptide (cyclized) is a synthetic peptide consisting of amino acids 96-110 of amyloid precursor peptide (APP) that is cyclized via a bridge between the cysteine residues at positions 3 and 10.
- GA21423 ent-[Amyloid β-Protein (20-16)]-β-Ala-D-Lys(ent-[Amyloid β-Protein (16-20)]) This all-D peptide contains two retro-inverso peptide klvff motifs of KLVFF (H-3682) corresponding to amino acids 16 to 20 of amyloid β-protein. The tandem dimer retro-inverso peptide showed about a 100-fold higher binding affinity (Kd = 1.3 . 10?² µM) for amyloid β-protein (1-40) fibrils than KLVFF (Kd = 1.1 ± 0.3 µM). It was also found to be more effective in preventing ordered fibril formation than the parent peptide KLVFF as judged by its increased ability to inhibit thioflavin T binding to β-sheet structures.
- GA20182 (Gln²²)-Amyloid β-Protein (1-40) The Dutch mutation (E22Q) of amyloid β-peptide aggregates more readily than the wild-type peptide and the resulting fibrils show increased neurotoxicity. The mutant peptide E22Q induced apoptosis of cerebral endothelial cells at a concentration of 25 μm, whereas WT Aβ 1-40 and the Italian mutant E22K (H-6698) showed no effect.
- GA20739 Amyloid β-Protein (1-6) amide Experiments using sub-peptides of Aβ42 revealed that the epitope identified by the antibody A8, as described by Ying and coworkers, lies within the 1-6 region of Aβ. The antibody displays high affinity for soluble Aβ42 oligomers in the molecular weight range of 16.5-25 kDa, and detected target antigen in brain sections from senescence-accelerated SAMP 8 mice. Amidated or acetylated and amidated forms of the sequence were used for example for quantitative structure retention relationships (QSRR) experiments. The latter could allow prediction of reversed-phase high-performance liquid chromatography (HPLC) retention of peptides, as reported by Kaliszan and coworkers.
- GA20727 Amyloid β-Protein (1-39) Small quantities of Aβ37, 38 and 39 can be detected in CSF together with Aβ40, the most abundant Aβ homolog, Aβ42, and N-terminally truncated amyloid peptides. The relative amounts depend on the variant of Alzheimer's disease. The C-terminally truncated amyloid peptides are also found in amyloid plaques.
- GA20720 Amyloid β-Protein (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.
- GA20535 Acetyl-Amyloid β-Protein (1-6) amide Experiments using sub-peptides of Aβ42 revealed that the epitope identified by the antibody A8, as described by Ying and coworkers, lies within the 1-6 region of Aβ. The antibody displays high affinity for soluble Aβ42 oligomers in the molecular weight range of 16.5-25 kDa, and detected target antigen in brain sections from senescence-accelerated SAMP 8 mice. Amidated or acetylated and amidated forms of the sequence were used for example for quantitative structure retention relationships (QSRR) experiments. The latter could allow prediction of reversed-phase high-performance liquid chromatography (HPLC) retention of peptides, as reported by Kaliszan and coworkers.
- GA20533 Acetyl-Amyloid β/A4 Protein Precursor₇₇₀ (96-110) (cyclized) 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.
- GA20526 Acetyl-(Pro¹⁸,Asp²¹)-Amyloid β-Protein (17-21) amide The pentapeptide Ac-LPFFD-NH? (iAβ5p) is an analog of product H-4876 with small chemical modifications which enhance its stability against proteolytic degradation. iAβ5p acts as a β-sheet breaker peptide and crosses the blood-brain barrier at a higher rate than most proteins and peptides known to be selectively taken up by the brain so that it is assumed that the peptide is being specifically transported to the brain. A significant increase in neuronal survival and decrease in brain inflammation associated with the reduction of amyloid plaques in two different transgenic Alzheimer`s disease (AD) models is additionally reported for iAβ5p.
- GA20284 (Pyr³)-Amyloid β-Protein (3-42) (Pyr³)-Amyloid β-Protein (3-42) was found to be the predominant amyloid β-peptide structure deposited in human brain of Alzheimer's disease and Down's syndrome patients. Therefore, (Pyr³)-Aβ (3-42) is suggested to accumulate in the brain and to trigger the formation of insoluble amyloid β-peptide deposits. Nussbaum et al. studies the Prion-like behaviour and tau-dependent cytotoxicity of the truncated Aβ sequence.
- GA20030 (Arg⁶)-Amyloid β-Protein (1-40) The English (H6R) mutation of β-amyloid peptides accelerates fibrillation without increasing protofibril formation. Ono et al. showed that the English and Tottori mutations alter Abeta assembly at its earliest stages, monomer folding and oligomerization, and produce oligomers that are more toxic to cultured neuronal cells than are wild type oligomers. The exchange of His? by Arg influences the structure of the Cu(II) complex formed by Aβ peptides.
- GA20024 (7-Diethylaminocoumarin-3-yl)carbonyl-Amyloid β-Protein (1-40) 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.
- GC16243 β-Amyloid (1-42), human TFA β-Amyloid (1-42), human TFA (Amyloid β-Peptide (1-42) (human) TFA)는 알츠하이머병의 발병기전에 중요한 역할을 하는 42-아미노산 펩타이드입니다.
- GA23601 Teplow's Amyloid β-Protein (1-42) (scrambled II) This peptide is a specifically designed negative control in studies with Abeta42. It is "scrambled", which means it contains the same amino acids as Abeta42, but in different order. Referring to studies by Yamin and coworkers, Teplow's Amyloid β-Protein (1-42) does not show a number of phenomena regularly observed with Abeta42 (fibril formation, oligomerization, toxicity to neurons) and furthermore has a relatively flat hydropathy profile, which can be an advantage in several studies, for example in order to avoid unspecific interaction with the cell membrane.
- GA23600 Teplow's Amyloid β-Protein (1-40) (scrambled II) This peptide is a specifically designed negative control in studies with Abeta40. It is "scrambled", which means it contains the same amino acids as Abeta40, but in different order. Referring to studies by Yamin and coworkers, Teplow's Amyloid β-Protein (1-40) does not show a number of phenomena regularly observed with Abeta40 (fibril formation, oligomerization, toxicity to neurons) and furthermore has a relatively flat hydropathy profile, which can be an advantage in several studies, for example in order to avoid unspecific interaction with the cell membrane.
- GA23175 Mca-Amyloid β/A4 Protein Precursor₇₇₀ (667-676)-Lys(Dnp)-Arg-Arg amide 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.
- GA21424 ent-Amyloid β-Protein (1-42) All-D Aβ (1-42) exhibits similar properites as the all-L Aβ. The peptide forms ion channels in lipid bilayers.
- GA20748 Amyloid β-Protein (3-42) The N-terminally truncated Aβ42 may be formed in increased amounts as AD progresses. Aβ 3-42 is the precursor of the Pyr-peptide. (Pyr³)-Aβ 3-42 positive plaques are resistant to age-dependent degradation likely due to their high stability and propensity to aggregate.
- GA20745 Amyloid β-Protein (25-35) amide The amidation of amyloid β-protein (25-35) leads to a product in which the amyloidogenic capacity of amyloid β-protein (25-35) has been strongly reduced, while the neurotoxic activity was found to be independent of the aggregated state of the peptide.
- GA20744 Amyloid β-Protein (2-42) Aβ 2-42 could be a biomarker for differentiating AD from other degenerative dementias, such as frontotemporal dementias (FTD). The peptide promotes phagocytosis by macrophages.
- GA20742 Amyloid β-Protein (17-40) Cleavage of APP by alpha- and gamma-secretase (i.e. the non-amyloidogenic pathway) yields p3 peptide, a mix of Aβ 17-40 and Aβ 17-42. p3 is a major constituent of diffuse plaques observed in AD brains and pre-amyloid plaques in people affected by Down syndrome.
- GA20738 Amyloid β-Protein (1-6) Experiments using sub-peptides of Aβ42 revealed that the epitope identified by the antibody A8, as described by Ying and coworkers, lies within the 1-6 region of Aβ. The antibody displays high affinity for soluble Aβ42 oligomers in the molecular weight range of 16.5-25 kDa, and detected target antigen in brain sections from senescence-accelerated SAMP 8 mice.
- GA20722 Amyloid β-Protein (1-14) The N-terminal Aβ fragments Aβ1-14, Aβ1-15 (H-6368), and Aβ1-16 (H-2958) are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The presence of these small peptides is consistent with a catabolic amyloid precursor protein cleavage pathway by β- followed by α-secretase. It has been shown that Aβ1-14, Aβ1-15, and Aβ1-16 increase dose-dependently in response to γ-secretase inhibitor treatment while Aβ1-42 levels are unchanged.
- GA20718 Amyloid β/A4 Protein Precursor₇₇₀ (667-676) The peptide substrate APP (667-676), SEVKMDAEFR, corresponds to the wild-type amyloid precursor protein (APP) β-secretase cleavage site. SEVKMDAEFR has been used for assaying β-secretase activity.
- GA20534 Acetyl-Amyloid β-Protein (15-20) amide Incubation of Ac-QKLVFF-NH? with the amyloid β-protein (1-40) inhibited polymerization of the amyloid β-protein (1-40) into amyloid fibrils. The peptide is thought to block the polymerization sites.
- GA20283 (Pyr³)-Amyloid β-Protein (3-40) The pyroglutamate-modified amyloid-β peptides derived from Aβ40 (H-7422) and Aβ42 (H-4796) have gained considerable attention as potential key participants in the pathology of Alzheimer's disease (AD) due to their abundance in AD brain, high aggregation propensity, stability, and cellular toxicity. Aβ40 and 42 can be N-terminally truncated by action of cathepsin B. The cyclization of Glu³ is catalyzed by glutaminyl cyclase. Hence, inhibition of these enzymes could be a therapeutic approach to AD.
- GA20282 (Pyr¹¹)-Amyloid β-Protein (11-40) pEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV, the N-terminally truncated isoform of the amyloid β-protein (Aβ) beginning with a pyroglutamate (Pyr) residue at position 11 was used in experiments studying the generality of fibrillogenesis-related helix formation. Comparing the fibrillogenesis kinetics of many of the most important clinically relevant amyloid β-protein alloforms it could be observed that among these peptides (Pyr¹¹)-amyloid β-protein (11-40) exhibited the greatest retardation of fibrillization rate.
- GA20259 (Nle³⁵)-Amyloid β-Protein (1-40) The reactive thioether of Met³? is crucial for the activity of Aβ 1-40 and Aβ 1-42. Due to the replacement of Met by inert Nle, M35Nle Aβ 1-40 was no longer toxic to cultured hippocampal neurons and had little effect on the level of protein carbonyl residues. The Nle peptide showed the same propensity to aggregate, whereas sulfoxide formation hindered the required conformational transition from random coil to β-sheet.
- GA20200 (Gly²²)-Amyloid β-Protein (1-42) The arctic mutant of amyloid β peptide 1-42, in which Glu²² is substituted by Gly, is distinctly more amyloidogenic than the wild-type Aβ 1-42.
- GA20197 (Gly²¹)-Amyloid β-Protein (1-40) Contrary to β-amyloid peptides mutated at position 22 (Dutch, Italian, Arctic mutants) the Flemish mutation (A21G) shows a decreased tendency to aggregate and a reduced neurotoxicity. In the studies of Betts and Tsubuki, A21G was degraded significantly more slowly by neprilysin than the wild-type Aβ 1-40 and the E22 mutants. The relative resistance to proteolytic degradation may account for the pathogenicity of the Aβ mutant.
- GA20184 (Gln²²,Asn²³)-Amyloid β-Protein (1-40) Transgenic mice expressing the vasculotropic Dutch/Iowa (E693Q/D694N) mutant human Aβ precursor protein in brain (Tg-SwDI) accumulate abundant cerebral microvascular fibrillar amyloid deposits and exhibit robust neuroinflammation. In vitro, the doubly mutated Aβ peptides showed an increased propensity to fibrillation and pathogenicity compared to the Dutch and Iowa single mutants.
- GA20050 (Cys⁰)-Amyloid β-Protein (1-40) Cys-Aβ1-40 can be easily and selectively modified, labeled, coupled to carriers e.g. by maleimide chemistry without affecting the sequences involved in fibril formation. The free mercapto moiety of the peptide adheres to gold surfaces.
- GA20042 (Asn⁷)-Amyloid β-Protein (1-40) The Tottori (D7N) mutation of β-amyloid peptides accelerates fibrillation without increasing protofibril formation. Ono et al. showed that the English and Tottori mutations alter Abeta assembly at its earliest stages, monomer folding and oligomerization, and produce oligomers that are more toxic to cultured neuronal cells than are wild type oligomers.
- GA20041 (Asn⁶⁷⁰,Sta⁶⁷¹,Val⁶⁷²)-Amyloid β/A4 Protein Precursor₇₇₀ (662-675) 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.
- GA20040 (Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-676) 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.
- GA20039 (Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675) 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.
- GA20029 (Arg¹³)-Amyloid β-Protein (1-40) H13R, a mutation in the metal-binding region of Abeta reduces its copper-mediated toxicity. The native rodent sequence containing an arginine at this position is more tolerant to metals than the human amyloid peptide.