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Amyloid β protein

Amyloid beta ( or Abeta) denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. The peptides derive from the amyloid precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ. Aβ molecules can aggregate to form flexible soluble oligomers which may exist in several forms. It is now believed that certain misfolded oligomers (known as "seeds") can induce other Aβ molecules to also take the misfolded oligomeric form, leading to a chain reaction akin to a prion infection. The oligomers are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold.

The normal function of Aβ is not well understood. Though some animal studies have shown that the absence of Aβ does not lead to any obvious loss of physiological function, several potential activities have been discovered for Aβ, including activation of kinase enzymes, protection against oxidative stress, regulation of cholesterol transport, functioning as a transcription factor, and anti-microbial activity (potentially associated with Aβ's pro-inflammatory activity).

The glymphatic system clears metabolic waste from the mammalian brain, and in particular amyloid beta. Indeed, a number of proteases have been implicated by both genetic and biochemical studies as being responsible for the recognition and degradation of amyloid beta; these include insulin degrading enzyme.and presequence protease. The rate of removal is significantly increased during sleep. However, the significance of the lymphatic system in Aβ clearance in Alzheimer's disease is unknown.

Targets for  Amyloid β protein

Products for  Amyloid β protein

  1. Cat.No. Product Name Information
  2. GA20740 Amyloid β-Protein (16-20) KLVFF corresponds to the minimum sequence binding the full-length amyloid β protein. The pentapeptide acts as a β-sheet breaker. Amyloid β-Protein (16-20)  Chemical Structure
  3. GA20741 Amyloid β-Protein (16-22) Self-assembling Aβ sequence. Amyloid β-Protein (16-22)  Chemical Structure
  4. 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. Amyloid β-Protein (17-40)  Chemical Structure
  5. 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. Amyloid β-Protein (2-42)  Chemical Structure
  6. GA20743 Amyloid β-Protein (20-29) FAEDVGSNKG. Amyloid β-Protein (20-29)  Chemical Structure
  7. 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. Amyloid β-Protein (25-35) amide  Chemical Structure
  8. GA20747 Amyloid β-Protein (3-40) Amyloid β-Protein (3-40)  Chemical Structure
  9. 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. Amyloid β-Protein (3-42)  Chemical Structure
  10. GA20746 Amyloid β-Protein (33-42) GLMVGGVVIA, a partial sequence of β-amyloid protein which is used for raising antibodies against Aβ 1-42. Li et al. studied the aggregation behavior of this and other Aβ 1-42 C-terminal fragments. Amyloid β-Protein (33-42)  Chemical Structure
  11. GA20749 Amyloid β-Protein (35-25) Reverse sequence of Aβ 25-35, inactive control. Amyloid β-Protein (35-25)  Chemical Structure
  12. GA20750 Amyloid β-Protein (36-38) Amyloid β-Protein (36-38)  Chemical Structure
  13. GA20751 Amyloid β-Protein (37-39) Amyloid β-Protein (37-39)  Chemical Structure
  14. GA20754 Amyloid β-Protein (4-42) Aβ 4-42 could be one of the earliest and most prominent Aβ species deposited in AD brain. Sequencing of amyloid plaque cores showed that 64% of the isolated Aβ had a phenylalanine at its N-terminus, and indeed, IP/MS experiments identified Aβ 4-42 as a major Aβ species in AD patients. Additionally, Aβ 4-42 was found to be a component of cotton wool plaques in familial AD patients with the V261I PS1 mutation. Aβ 4-42 was discovered as well in amyloid deposits from vascular dementia and familial Danish dementia patients. These observations indicate that Aβ 4-42 may contribute to the development of multiple CNS diseases. Amyloid β-Protein (4-42)  Chemical Structure
  15. GA20753 Amyloid β-Protein (40-1) Inactive control Amyloid β-Protein (40-1)  Chemical Structure
  16. GA20752 Amyloid β-Protein (40-1) Reverse sequence of Aβ 1-40. Amyloid β-Protein (40-1)  Chemical Structure
  17. GA20755 Amyloid β-Protein (5-42) Abeta 5-42 is produced from amyloid precursor protein by action of caspases. It is deposited in Alzheimer's disease brain as well, but less prone to aggregation. Amyloid β-Protein (5-42)  Chemical Structure
  18. GA20756 Amyloid β-Protein (6-20) Amyloid β-Protein (6-20)  Chemical Structure
  19. 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. Amyloid β/A4 Protein Precursor₇₇₀ (667-676)  Chemical Structure
  20. GA20719 Amyloid β/A4 Protein Precursor₇₇₀ (740-770) Amyloid β/A4 Protein Precursor??? (740-770) corresponds to a C-terminal amyloid precursor protein (APP) fragment known as C31. This fragment is intracellularly generated by proteolytic cleavage of APP by caspases-8 and -9. C31 had a proapoptotic and a cytotoxic effect on neuronal cells and was shown to be present in brains of Alzheimer's disease (AD) patients. In cultured cells caspase cleavage of APP was induced by amyloid β-protein and the subsequent generation of C31 contributed to the apoptotic cell death associated with amyloid β-protein. Amyloid precursor binding protein BP1 (APP-BP1) a cell cycle protein which is increased in AD brain was demonstrated to bind to the C31 region of APP and to mediate APP-induced apoptosis. Amyloid β/A4 Protein Precursor₇₇₀ (740-770)  Chemical Structure
  21. GP10118 Amyloid Beta-Peptide (1-40) (human)

    Amyloid β-Peptide (1-40) (human), (C194H295N53O58S1), a peptide with the sequence H2N-DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA-OH, MW= 4329.8. Amyloid beta (Aβ or Abeta) is a peptide of 36–43 amino acids that is processed from the Amyloid precursor protein.

    Amyloid Beta-Peptide (1-40) (human)  Chemical Structure
  22. GP10049 Amyloid Beta-Peptide (12-28) (human) Amyloid Beta-Peptide (12-28) (human)  Chemical Structure
  23. GP10082 Amyloid Beta-peptide (25-35) (human)

    Amyloid beta-peptide (25-35) (human) is an fragment of Alzheimer's Amyloid beta peptide which has neurotoxic effects.

    Amyloid Beta-peptide (25-35) (human)  Chemical Structure
  24. 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.

    Amyloid β-Peptide (1-42) human   Chemical Structure
  25. GP10057 Amyloid β-Peptide (10-20) (human) Amyloid β-Peptide (10-20) (human)  Chemical Structure
  26. GP10094 Amyloid β-peptide (10-35), amide Amyloid β-peptide (10-35), amide  Chemical Structure
  27. GP10097 Amyloid β-Protein (1-15) Amyloid β-Protein (1-15)  Chemical Structure
  28. GC45382 Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt)   Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  29. GC42798 Amyloid-β (1-38) Peptide (trifluoroacetate salt) Amyloid-β (1-38) (Aβ38) peptide is a fragment of the Aβ42 peptide. Amyloid-β (1-38) Peptide (trifluoroacetate salt)  Chemical Structure
  30. GC46850 Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt) A neuropeptide with diverse biological activities Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  31. GC46851 Amyloid-β (1-42) Peptide (trifluoroacetate salt) A 42-amino acid protein fragment of amyloid-β Amyloid-β (1-42) Peptide (trifluoroacetate salt)  Chemical Structure
  32. 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 . Amyloid-β (1-8) Peptide  Chemical Structure
  33. 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). Amyloid-β (1-8, A2V) Peptide  Chemical Structure
  34. 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. Amyloid-β (17-40) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  35. 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. Amyloid-β (17-42) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  36. 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. Amyloid-β (22-35) Peptide (trifluoroacetate salt)  Chemical Structure
  37. 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. Amyloid-β (25-35) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  38. 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. Amyloid-β (40-1) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  39. 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. Amyloid-β Precursor Protein (96-110) Peptide (cyclized) (human) (trifluoroacetate salt)  Chemical Structure
  40. GA20780 Arg-Glu(EDANS)-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (668-675)-Lys(DABCYL)-Arg 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. Arg-Glu(EDANS)-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (668-675)-Lys(DABCYL)-Arg  Chemical Structure
  41. GP10083 Beta-Amyloid (1-11) Beta-Amyloid (1-11)  Chemical Structure
  42. GC34232 Beta-Amyloid(1-14),mouse,rat Beta-Amyloid(1-14),mouse,rat  Chemical Structure
  43. GC40160 Biotin-Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt) Biotin-amyloid-β (1-28) peptide is a biotinylated peptide. Biotin-Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  44. 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. Biotin-Amyloid-β (1-40) Peptide (trifluoroacetate salt)  Chemical Structure
  45. 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. Biotin-Amyloid-β (1-42) Peptide (trifluoroacetate salt)  Chemical Structure
  46. GA20854 Biotinyl-εAhx-Amyloid β-Protein (1-40) The flexible LC spacer increases the accessibility of the biotin moiety. Biotinyl-εAhx-Amyloid β-Protein (1-40)  Chemical Structure
  47. GA20855 Biotinyl-εAhx-Amyloid β-Protein (1-42) The flexible LC spacer increases the accessibility of the biotin moiety. Biotinyl-εAhx-Amyloid β-Protein (1-42)  Chemical Structure
  48. GA20823 Biotinyl-Amyloid β-Protein (1-40) Biotinyl-Amyloid β-Protein (1-40) is a N-terminal-labelled biotinylated amyloid-ß-(1-40) peptide. Biotinyl-Amyloid β-Protein (1-40)  Chemical Structure
  49. GA20824 Biotinyl-Amyloid β-Protein (1-42) N-terminally biotin-labeled Aβ42. Biotinyl-Amyloid β-Protein (1-42)  Chemical Structure
  50. GA21351 Cys-Gly-His-Gly-Asn-Lys-Ser-Amyloid β-Protein (33-40) CGHGNKSGLMVGGVV. Cys-Gly-His-Gly-Asn-Lys-Ser-Amyloid β-Protein (33-40)  Chemical Structure
  51. GA21352 Cys-Gly-Lys-Arg-Amyloid β-Protein (1-42) Cys-Gly-Lys-Arg-Amyloid β-Protein (1-42)  Chemical Structure
  52. GA21353 Cys-Gly-Lys-Lys-Gly-Amyloid β-Protein (35-40) Cys-Gly-Lys-Lys-Gly-Amyloid β-Protein (35-40)  Chemical Structure
  53. 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. ent-Amyloid β-Protein (1-42)  Chemical Structure
  54. 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. ent-[Amyloid β-Protein (20-16)]-β-Ala-D-Lys(ent-[Amyloid β-Protein (16-20)])  Chemical Structure
  55. GC43650 FAM-Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt) FAM-Amyloid-β (1-40) peptide is a fluorescently labeled amyloid-β peptide. FAM-Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  56. GA21460 FITC-β-Ala-Amyloid β-Protein (1-40) FITC-β-Ala-Amyloid β-Protein (1-40)  Chemical Structure
  57. GA21461 FITC-β-Ala-Amyloid β-Protein (1-42) FITC-β-Ala-Amyloid β-Protein (1-42)  Chemical Structure
  58. GA21462 FITC-εAhx-Amyloid β-Protein (1-42) FITC-εAhx-Amyloid β-Protein (1-42)  Chemical Structure
  59. GC45465 Glp-Amyloid-β (3-40) Peptide (human) (trifluoroacetate salt) Glp-Amyloid-β (3-40) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  60. GA23171 Mca-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675)-Lys(Dnp) Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site of the Swedish mutation of APP, SEVNLDAEF. Mca-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675)-Lys(Dnp)  Chemical Structure
  61. GA23172 Mca-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675)-Lys(Dnp) amide Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site of the Swedish mutation of APP. The kinetic parameters of Mca-SEVNLDAEFK(Dnp) amide at pH 4.5 are Km = 4.5 µM and kcat = 0.25 min?¹. Mca-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675)-Lys(Dnp) amide  Chemical Structure
  62. 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. Mca-Amyloid β/A4 Protein Precursor₇₇₀ (667-676)-Lys(Dnp)-Arg-Arg amide  Chemical Structure
  63. GA23270 N-Me-Abz-Amyloid β/A4 Protein Precursor₇₇₀ (708-715)-Lys(Dnp)-D-Arg-D-Arg-D-Arg amide 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. N-Me-Abz-Amyloid β/A4 Protein Precursor₇₇₀ (708-715)-Lys(Dnp)-D-Arg-D-Arg-D-Arg amide  Chemical Structure
  64. GC44986 TAMRA-Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt) TAMRA-Amyloid-β (1-28) peptide is a fluorescently labeled peptide. TAMRA-Amyloid-β (1-28) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  65. GC40128 TAMRA-Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt) TAMRA-Amyloid-β (1-40) peptide is a fluorescently labeled peptide. TAMRA-Amyloid-β (1-40) Peptide (human) (trifluoroacetate salt)  Chemical Structure
  66. GC44987 TAMRA-Amyloid-β (1-42) Peptide (trifluoroacetate salt) TAMRA-Amyloid-β (1-42) peptide is a fluorescently labeled peptide. TAMRA-Amyloid-β (1-42) Peptide (trifluoroacetate salt)  Chemical Structure
  67. 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. Teplow's Amyloid β-Protein (1-40) (scrambled II)  Chemical Structure
  68. 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. Teplow's Amyloid β-Protein (1-42) (scrambled II)  Chemical Structure
  69. GA23614 Tide Fluor™ 5WS-Amyloid β-Protein (1-40) Fluorescent dye-labeled Aβ40, excitation at 649 nm, emission at 664 nm. Tide Fluor™ 5WS shows strong fluorescence and excellent photostability. Tide Fluor™ 5WS-Amyloid β-Protein (1-40)  Chemical Structure
  70. GA23616 Tide Fluor™ 7WS-Amyloid β-Protein (1-40) Fluorescent dye-labeled Aβ40, excitation at 749nm, emission at 775nm. Tide Fluor™ 7WS shows strong fluorescence and excellent photostability. Tide Fluor™ 7WS-Amyloid β-Protein (1-40)  Chemical Structure
  71. GC16243 β-Amyloid (1-42), human TFA

    Amyloid β-Peptide (1-42) human TFA is a 42-amino acid peptide.

    β-Amyloid (1-42), human TFA  Chemical Structure

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