Amyloid β protein
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Amyloid beta (Aβ 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.
Products Related to Amyloid β protein(166)
- GA21424ent-Amyloid β-Protein (1-42)CAS: 342896-25-7Purity: >98%
All-D Aβ (1-42) exhibits similar properites as the all-L Aβ. The peptide forms ion channels in lipid bilayers.
- GA23171Mca-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675)-Lys(Dnp)CAS: 1802078-31-4Purity: >98%
Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site of the Swedish mutation of APP, SEVNLDAEF.
- GA23175Mca-Amyloid β/A4 Protein Precursor₇₇₀ (667-676)-Lys(Dnp)-Arg-Arg amideCAS: 1802078-33-6Purity: >98%
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.
- GA23270N-Me-Abz-Amyloid β/A4 Protein Precursor₇₇₀ (708-715)-Lys(Dnp)-D-Arg-D-Arg-D-Arg amideCAS: 600728-90-3Purity: >98%
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.
- GA23600Teplow's Amyloid β-Protein (1-40) (scrambled II)CAS: 1987844-71-2Purity: >98%
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.
- GA23601Teplow's Amyloid β-Protein (1-42) (scrambled II)CAS: 1987844-92-7Purity: >98%
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.
- GA23614Tide Fluor™ 5WS-Amyloid β-Protein (1-40)Purity: >98%
Fluorescent dye-labeled Aβ40, excitation at 649 nm, emission at 664 nm. Tide Fluor™ 5WS shows strong fluorescence and excellent photostability.
- GA23616Tide Fluor™ 7WS-Amyloid β-Protein (1-40)Purity: >98%
Fluorescent dye-labeled Aβ40, excitation at 749nm, emission at 775nm. Tide Fluor™ 7WS shows strong fluorescence and excellent photostability.
- GC16243β-Amyloid (1-42), human TFACAS: 107761-42-2Purity: >99.00%
β-Amyloid (1-42), human TFA is a 42-amino acid peptide.
- GC18339Amyloid β-Peptide (1-42) humanCAS: 107761-42-2Purity: >98.00%
Amyloid β-Peptide (1-42) human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.
- GC30325β-Amyloid 22-35 (Amyloid β-Protein (22-35))CAS: 144189-71-9Purity: >98%
β-Amyloid 22-35 (Amyloid β-Protein (22-35)) is a 14-amino acid peptide fragment that can spontaneously aggregate to form β-sheet structures and exerts significant cytotoxicity on hippocampal neurons.
- GC31129β-Amyloid 1-16 (Amyloid β-Protein (1-16))CAS: 131580-10-4Purity: >98.50%
β-Amyloid 1-16 (Amyloid β-Protein (1-16)) is a β-Amyloid protein fragment that can bind to copper(II) ions.
- GC31137β-Amyloid 29-40 (Amyloid beta-protein(29-40))CAS: 184865-04-1Purity: >98%
β-Amyloid 29-40 (Amyloid beta-protein(29-40)) is a fragment of Amyloid-β peptide.
- GC31146β-Amyloid (10-35), amideCAS: 181427-66-7Purity: >98%
β-Amyloid (10-35), amide is composed of 26 aa (10-35 residues of the Aβ peptide) and is the primary component of the amyloid plaques of Alzheimer's disease.
- GC31171β-Amyloid 1-28 (Amyloid β-Protein (1-28))CAS: 109770-29-8Purity: >98%
β-Amyloid 1-28 (Amyloid β-Protein (1-28)) is a β-Amyloid protein fragment involved in metal binding.
- GC31179β-Amyloid 31-35CAS: 149385-65-9Purity: >99.50%
β-Amyloid 31-35 is the shortest sequence of native Amyloid-β peptide that retains neurotoxic activity.
- GC35334Amyloid β Peptide (42-1)(human)CAS: 317366-82-8Purity: >98%
Amyloid β Peptide (42-1)(human) is the inactive form of Amyloid β Peptide (1-42).
- GC35335Amyloid β-peptide (1-40) ratCAS: 144409-98-3Purity: >98%
Amyloid β-peptide (1-40) rat is a rat form of the amyloid β-peptide, which accumulates as an insoluble extracellular deposit around neurons, giving rise to the senile plaques associated with Alzheimer's disease (AD).
| Catalog No. | Product Name | CAS No. | Purity | Structure |
|---|---|---|---|---|
| GA21424 | ent-Amyloid β-Protein (1-42) | 342896-25-7 | >98% | |
All-D Aβ (1-42) exhibits similar properites as the all-L Aβ. The peptide forms ion channels in lipid bilayers. | ||||
| GA21460 | FITC-β-Ala-Amyloid β-Protein (1-40) | 1802087-76-8 | >98% | |
| GA21461 | FITC-β-Ala-Amyloid β-Protein (1-42) | 1802087-77-9 | >98% | |
| GA21462 | FITC-εAhx-Amyloid β-Protein (1-42) | - | >98% | |
| GA23171 | Mca-(Asn⁶⁷⁰,Leu⁶⁷¹)-Amyloid β/A4 Protein Precursor₇₇₀ (667-675)-Lys(Dnp) | 1802078-31-4 | >98% | |
Fluorogenic (FRET) substrate for pro-memapsin-2 containing the β-secretase site of the Swedish mutation of APP, SEVNLDAEF. | ||||
| GA23175 | Mca-Amyloid β/A4 Protein Precursor₇₇₀ (667-676)-Lys(Dnp)-Arg-Arg amide | 1802078-33-6 | >98% | |
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. | ||||
| GA23270 | N-Me-Abz-Amyloid β/A4 Protein Precursor₇₇₀ (708-715)-Lys(Dnp)-D-Arg-D-Arg-D-Arg amide | 600728-90-3 | >98% | |
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. | ||||
| GA23600 | Teplow's Amyloid β-Protein (1-40) (scrambled II) | 1987844-71-2 | >98% | |
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. | ||||
| GA23601 | Teplow's Amyloid β-Protein (1-42) (scrambled II) | 1987844-92-7 | >98% | |
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. | ||||
| GA23614 | Tide Fluor™ 5WS-Amyloid β-Protein (1-40) | - | >98% | |
Fluorescent dye-labeled Aβ40, excitation at 649 nm, emission at 664 nm. Tide Fluor™ 5WS shows strong fluorescence and excellent photostability. | ||||
| GA23616 | Tide Fluor™ 7WS-Amyloid β-Protein (1-40) | - | >98% | |
Fluorescent dye-labeled Aβ40, excitation at 749nm, emission at 775nm. Tide Fluor™ 7WS shows strong fluorescence and excellent photostability. | ||||
| GC16243 | β-Amyloid (1-42), human TFA | 107761-42-2 | >99.00% | |
β-Amyloid (1-42), human TFA is a 42-amino acid peptide. | ||||
| GC18339 | Amyloid β-Peptide (1-42) human | 107761-42-2 | >98.00% | |
Amyloid β-Peptide (1-42) human is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease. | ||||
| GC30325 | β-Amyloid 22-35 (Amyloid β-Protein (22-35)) | 144189-71-9 | >98% | |
β-Amyloid 22-35 (Amyloid β-Protein (22-35)) is a 14-amino acid peptide fragment that can spontaneously aggregate to form β-sheet structures and exerts significant cytotoxicity on hippocampal neurons. | ||||
| GC31129 | β-Amyloid 1-16 (Amyloid β-Protein (1-16)) | 131580-10-4 | >98.50% | |
β-Amyloid 1-16 (Amyloid β-Protein (1-16)) is a β-Amyloid protein fragment that can bind to copper(II) ions. | ||||
| GC31137 | β-Amyloid 29-40 (Amyloid beta-protein(29-40)) | 184865-04-1 | >98% | |
β-Amyloid 29-40 (Amyloid beta-protein(29-40)) is a fragment of Amyloid-β peptide. | ||||
| GC31146 | β-Amyloid (10-35), amide | 181427-66-7 | >98% | |
β-Amyloid (10-35), amide is composed of 26 aa (10-35 residues of the Aβ peptide) and is the primary component of the amyloid plaques of Alzheimer's disease. | ||||
| GC31171 | β-Amyloid 1-28 (Amyloid β-Protein (1-28)) | 109770-29-8 | >98% | |
β-Amyloid 1-28 (Amyloid β-Protein (1-28)) is a β-Amyloid protein fragment involved in metal binding. | ||||
| GC31179 | β-Amyloid 31-35 | 149385-65-9 | >99.50% | |
β-Amyloid 31-35 is the shortest sequence of native Amyloid-β peptide that retains neurotoxic activity. | ||||
| GC34232 | Beta-Amyloid(1-14),mouse,rat | - | >98% | |
| GC34242 | β-Amyloid (1-42), rat TFA | - | >98% | |
| GC34391 | β-Amyloid 15-21 (Beta-Amyloid (15-21)) | - | >98% | |
| GC35334 | Amyloid β Peptide (42-1)(human) | 317366-82-8 | >98% | |
Amyloid β Peptide (42-1)(human) is the inactive form of Amyloid β Peptide (1-42). | ||||
| GC35335 | Amyloid β-peptide (1-40) rat | 144409-98-3 | >98% | |
Amyloid β-peptide (1-40) rat is a rat form of the amyloid β-peptide, which accumulates as an insoluble extracellular deposit around neurons, giving rise to the senile plaques associated with Alzheimer's disease (AD). | ||||