SensoLyte® 520 β-Secretase, BACE2, ADAM 10 or Neprilysin activity assay kits:
- One-step homogeneous assays
- 간편한 실험 방식 (mix-and-read format)
- FRET peptide (5-FAM / QXLTM520) 형광 측정방식으로 높은 민감도
- 범용적인 파장대로 흡광도 측정
β-Amyloid ELISA kits (human, mouse/rat)
- Convenient Format
Pre-coated 와 pre-blocked 96-well 제공
실험에 필요한 시약들을 하나의 kit로 제공
실온에서 1시간의 분석 시간 (incubation 시간 제외)
- Minimal Sample Size
소량의 샘플 (10 ~20ul)로 실험 가능
- High Sensitivity
2pg/ml (13fmoles/ml) 도 detection 가능한 높은 민감도
Citations
Hidisoglu E, Yargicoglu P. (2020). Auditory evoked potentials might have the potential to serve as early indicators related to amyloid beta peptide toxicity. Advances in Medical Sciences. 65(1):223-32. DOI: 10.1016/j.advms.2020.02.001
Bertoldi, K. et al. (2018). Circulating extracellular vesicles in the aging process: impact of aerobic exercise. Mol Cell Biochem. 440, 115–125. DOI:10.1007/s11010-017-3160-4.
Yang H, et al. (2018). The effect of chronic cerebral hypoperfusion on amyloid-β metabolism in a transgenic mouse model of Alzheimer's disease (PS1V97L). Journal of Alzheimer's Disease. 62(4):1609-21. DOI:10.3233/JAD-171094.
Mohamed LA, et al. (2016). Role of P-glycoprotein in mediating rivastigmine effect on amyloid-β brain load and related pathology in Alzheimer's disease mouse model. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease. 1862(4):778-87.
Camponova P, et al. (2017). Alteration of high-density lipoprotein functionality in Alzheimer's disease patients. Canadian Journal of Physiology and Pharmacology. 95(8):894-903. DOI:10.1139/cjpp-2016-0710.
Zhang, J. et al. (2014). Synaptic and cognitive improvements by inhibition of 2-AG metabolism are through upregulation of microRNA-188-3p in a mouse model of Alzheimer's Disease. J Neurosci. 34, 14919. DOI: 10.1523/JNEUROSCI.1165-14.2014.
Qosa H, et al. (2014). Differences in amyloid-β clearance across mouse and human blood-brain barrier models: kinetic analysis and mechanistic modeling. Neuropharmacol. 79:668-678. DOI:10.1016/j.neuropharm.2014.01.023
The SensoLyte® 520 Acetylcholinesterase Assay Kit is a homogeneous assay that can be used to detect the activity of enzyme and for screening of AChE inhibitors. Active AChE generates fluorescence that can be monitored at excitation/emission=490/520 nm. The long wavelength fluorescence of the substrate in this kit minimizes interference from autofluorescence of components in biological samples and test compounds, resulting in higher sensitivity.
TACE (tumor necrosis factor-alpha converting enzyme), α-secretase, or ADAM17 is a member of the ADAM family of proteases that contain both disintegrin and metalloprotease (catalytic) domains. This enzyme is involved in sperm-egg binding and fusion, muscle cell fusion, neurogenesis, modulation of Notch receptor and ligand processing, and processing of the pro-inflammatory cytokine, TNFα. TACE is currently being explored as a target for anti-inflammatory drugs.
BACE2 (β-Secretase-2, Memapsin-1) belongs to the family of transmembrane aspartic proteases. BACE2 has approximately 75% homology with BACE1 (β-Secretase-1) and is similar in that both cleaves Amyloid Precursor Protein (APP) at β-site generating N-terminal part of beta-Amyloid peptide. Unlike BACE1 that is highly expressed in pancreas and brain tissue, BACE2 is more widespread and can be found in many peripheral tissues at higher levels compared to BACE1. BACE2 is one of the highest efficiency beta-amyloid peptide degrading enzyme that is less active only to insulin degrading enzyme (IDE); therefore, targeting BACE2 is considered a potential therapeutic strategy for the prevention and treatment of Alzheimer's disease.
BACE1 (β-Secretase) is a membrane-anchored aspartic protease existing in acidic subcellular vesicles. It is a key player in producing β-amyloid peptides through proteolytic cleavage of the β-amyloid precursor protein (APP). Accumulation of neurotoxic β-amyloid peptide is seen in senile plaques in the brains of patients with Alzheimer’s disease (AD), an age-related cognitive disorder. Therefore, targeting β-secretase is considered a potential therapeutic strategy for the prevention and treatment of AD.
The SensoLyte® 520 ADAM10 Activity Assay Kit is an optimized assay that can be used to detect the ADAM 10 activity. The unique FRET substrate contained in the kit was designed to reduce the cross reactivity with ADAM17 (also called tumor necrosis factor-α-converting enzyme, TACE). When active ADAM10 cleaves the FRET substrate, it results in an increase of 5-FAM fluorescence monitored at excitation/emission = 490/520 nm. The long wavelength fluorescence of 5-FAM is also less interfered by the autofluorescence of components in biological samples and test compounds. This assay can detect as low as 0.25 ng/mL active ADAM10.
This SensoLyte® high-sensitivity (2 pg/ml) beta-Amyloid (1-40) Quantitative ELISA Kit (Human) provides a convenient and quantitative assay for determining human beta-Amyloid (1-40) (Aβ40) amount in cell and tissue lysate as well as in body fluids. Compared to other anti-human Aβ40 ELISA kits on the market, it takes less time to run this assay. HRP conjugated detection antibody in this kit is added simultaneously with samples and standards during the assay. This eliminates extra incubation and washing steps and makes this kit one-step procedure for Aβ40 quantification.
This SensoLyte® high-sensitivity (2 pg/ml) beta-Amyloid (1-42) Quantitative ELISA Kit (Human) provides a convenient and quantitative assay for determining human beta-Amyloid (1-42) (Aβ42) amount in cell and tissue lysate as well as in body fluids. Compared to other anti-human Aβ42 ELISA kits on the market, it takes less time to run this assay. HRP conjugated detection antibody in this kit is added simultaneously with samples and standards during the assay. This eliminates extra incubation and washing steps and makes this kit one-step procedure for Aβ42 quantification.
SensoLyte® Thioflavin T β-Amyloid (1-42) Aggregation Kit
1 KIT
Anaspec
The SensoLyte® ThT β-Amyloid (1-42) Aggregation kit provides a convenient and standard method to measure Aβ42 aggregation using Thioflavin T dye. Aβ42 peptide is pretreated to ensure it is in a monomeric state. An optimized fibrillation buffer is included with the kit, and two known inhibitors are supplied as controls. The assay is based on the property of ThT dye in which fluorescence (Ex/Em=440/484 nm) is increased when bound to aggregated Aβ peptides. Alzheimer's disease (AD), the most common cause of dementia, is characterized by the presence of senile plaques and neurofibrillary tangles, surrounded by damaged neurons. Beta-Amyloid (Aβ) peptides, Aβ40 (1-40) and Aβ42 (1-42), were found to be a major component of the above plaques. Many studies suggest that these peptides can form toxic oligomers and fibrils under physiological conditions and rapidly aggregate. Since Aβ aggregation is evidently an essential event in the pathogenesis of AD, a reliable assay is important to study Aβ fibrillation kinetics and screen for Aβ aggregation inhibitors.
SensoLyte® Thioflavin T β-Amyloid (1-40) Aggregation Kit
1 KIT
Anaspec
The SensoLyte® ThT β-Amyloid (1-40) Aggregation kit provides a convenient and standard method to measure Aβ40 aggregation using Thioflavin T dye. Aβ40 peptide is pretreated to ensure it is in a monomeric state. An optimized fibrillation buffer is included with the kit, and two known inhibitors are supplied as controls. The assay is based on the property of ThT dye in which fluorescence (Ex/Em=440/484 nm) is increased when bound to aggregated Aβ peptides. Alzheimer's disease (AD), the most common cause of dementia, is characterized by the presence of senile plaques and neurofibrillary tangles, surrounded by damaged neurons. Beta-Amyloid (Aβ) peptides, Aβ40 (1-40) and Aβ42 (1-42), were found to be a major component of the above plaques. Many studies suggest that these peptides can form toxic oligomers and fibrils under physiological conditions and rapidly aggregate. Since Aβ aggregation is evidently an essential event in the pathogenesis of AD, a reliable assay is important to study Aβ fibrillation kinetics and screen for Aβ aggregation inhibitors.
Neprilysin (NEP) is a transmembrane metallopeptidase normally expressed by a variety of tissues. It is also known as neutral endopeptidase, and enkephalinase. NEP cleaves peptides at the N-terminal side of hydrophobic amino acid residues and is responsible for the degradation and inactivation of a variety of physiological substrates. NEP is a major extracellular amyloid beta-peptide degrading enzyme in the brain and targeting NEP is considered a potential therapeutic strategy for the prevention and treatment of Alzheimer's disease. NEP has also been implicated in the pathogenesis of hypertension, diabetes, and cancer. The SensoLyte® 520 Neprilysin Assay Kit employs a novel internally quenched 5-FAM/QXL® FRET substrate for the detection of neprilysin activity. The enzyme cleaves the FRET substrate into two separate fragments resulting in the release of 5-FAM fluorescence, which can be monitored at excitation /emission= 490/520 nm. The long wavelength fluorescence of 5-FAM is less interfered by the autofluorescence of components in biological samples and test compounds. The assay can detect as low as 0.78 ng/mL of active Neprilysin.
The SensoLyte® Green Pin1 Assay Kit uses a fluorogenic substrate in the cis isoform. Pin1 changes substrate into trans conformation, which is then readily cleaved to generate fluorescent signal which can be monitored at Ex/Em=490/520nm. Increase in fluorescence intensity is directly proportional to the Pin1 activity.
The SensoLyte® 520 Acetylcholinesterase Assay Kit is a homogeneous assay that can be used to detect the activity of enzyme and for screening of AChE inhibitors. Active AChE generates fluorescence that can be monitored at excitation/emission=490/520 nm. The long wavelength fluorescence of the substrate in this kit minimizes interference from autofluorescence of components in biological samples and test compounds, resulting in higher sensitivity.
TACE (tumor necrosis factor-alpha converting enzyme), α-secretase, or ADAM17 is a member of the ADAM family of proteases that contain both disintegrin and metalloprotease (catalytic) domains. This enzyme is involved in sperm-egg binding and fusion, muscle cell fusion, neurogenesis, modulation of Notch receptor and ligand processing, and processing of the pro-inflammatory cytokine, TNFα. TACE is currently being explored as a target for anti-inflammatory drugs.
BACE2 (β-Secretase-2, Memapsin-1) belongs to the family of transmembrane aspartic proteases. BACE2 has approximately 75% homology with BACE1 (β-Secretase-1) and is similar in that both cleaves Amyloid Precursor Protein (APP) at β-site generating N-terminal part of beta-Amyloid peptide. Unlike BACE1 that is highly expressed in pancreas and brain tissue, BACE2 is more widespread and can be found in many peripheral tissues at higher levels compared to BACE1. BACE2 is one of the highest efficiency beta-amyloid peptide degrading enzyme that is less active only to insulin degrading enzyme (IDE); therefore, targeting BACE2 is considered a potential therapeutic strategy for the prevention and treatment of Alzheimer's disease.
BACE1 (β-Secretase) is a membrane-anchored aspartic protease existing in acidic subcellular vesicles. It is a key player in producing β-amyloid peptides through proteolytic cleavage of the β-amyloid precursor protein (APP). Accumulation of neurotoxic β-amyloid peptide is seen in senile plaques in the brains of patients with Alzheimer’s disease (AD), an age-related cognitive disorder. Therefore, targeting β-secretase is considered a potential therapeutic strategy for the prevention and treatment of AD.
The SensoLyte® 520 ADAM10 Activity Assay Kit is an optimized assay that can be used to detect the ADAM 10 activity. The unique FRET substrate contained in the kit was designed to reduce the cross reactivity with ADAM17 (also called tumor necrosis factor-α-converting enzyme, TACE). When active ADAM10 cleaves the FRET substrate, it results in an increase of 5-FAM fluorescence monitored at excitation/emission = 490/520 nm. The long wavelength fluorescence of 5-FAM is also less interfered by the autofluorescence of components in biological samples and test compounds. This assay can detect as low as 0.25 ng/mL active ADAM10.
This SensoLyte® high-sensitivity (2 pg/ml) beta-Amyloid (1-40) Quantitative ELISA Kit (Human) provides a convenient and quantitative assay for determining human beta-Amyloid (1-40) (Aβ40) amount in cell and tissue lysate as well as in body fluids. Compared to other anti-human Aβ40 ELISA kits on the market, it takes less time to run this assay. HRP conjugated detection antibody in this kit is added simultaneously with samples and standards during the assay. This eliminates extra incubation and washing steps and makes this kit one-step procedure for Aβ40 quantification.
This SensoLyte® high-sensitivity (2 pg/ml) beta-Amyloid (1-42) Quantitative ELISA Kit (Human) provides a convenient and quantitative assay for determining human beta-Amyloid (1-42) (Aβ42) amount in cell and tissue lysate as well as in body fluids. Compared to other anti-human Aβ42 ELISA kits on the market, it takes less time to run this assay. HRP conjugated detection antibody in this kit is added simultaneously with samples and standards during the assay. This eliminates extra incubation and washing steps and makes this kit one-step procedure for Aβ42 quantification.
SensoLyte® Thioflavin T β-Amyloid (1-42) Aggregation Kit
Cat No.
ANA-AS-72214
규격
1 KIT
제조사
Anaspec
제품정보
The SensoLyte® ThT β-Amyloid (1-42) Aggregation kit provides a convenient and standard method to measure Aβ42 aggregation using Thioflavin T dye. Aβ42 peptide is pretreated to ensure it is in a monomeric state. An optimized fibrillation buffer is included with the kit, and two known inhibitors are supplied as controls. The assay is based on the property of ThT dye in which fluorescence (Ex/Em=440/484 nm) is increased when bound to aggregated Aβ peptides. Alzheimer's disease (AD), the most common cause of dementia, is characterized by the presence of senile plaques and neurofibrillary tangles, surrounded by damaged neurons. Beta-Amyloid (Aβ) peptides, Aβ40 (1-40) and Aβ42 (1-42), were found to be a major component of the above plaques. Many studies suggest that these peptides can form toxic oligomers and fibrils under physiological conditions and rapidly aggregate. Since Aβ aggregation is evidently an essential event in the pathogenesis of AD, a reliable assay is important to study Aβ fibrillation kinetics and screen for Aβ aggregation inhibitors.
SensoLyte® Thioflavin T β-Amyloid (1-40) Aggregation Kit
Cat No.
ANA-AS-72213
규격
1 KIT
제조사
Anaspec
제품정보
The SensoLyte® ThT β-Amyloid (1-40) Aggregation kit provides a convenient and standard method to measure Aβ40 aggregation using Thioflavin T dye. Aβ40 peptide is pretreated to ensure it is in a monomeric state. An optimized fibrillation buffer is included with the kit, and two known inhibitors are supplied as controls. The assay is based on the property of ThT dye in which fluorescence (Ex/Em=440/484 nm) is increased when bound to aggregated Aβ peptides. Alzheimer's disease (AD), the most common cause of dementia, is characterized by the presence of senile plaques and neurofibrillary tangles, surrounded by damaged neurons. Beta-Amyloid (Aβ) peptides, Aβ40 (1-40) and Aβ42 (1-42), were found to be a major component of the above plaques. Many studies suggest that these peptides can form toxic oligomers and fibrils under physiological conditions and rapidly aggregate. Since Aβ aggregation is evidently an essential event in the pathogenesis of AD, a reliable assay is important to study Aβ fibrillation kinetics and screen for Aβ aggregation inhibitors.
Neprilysin (NEP) is a transmembrane metallopeptidase normally expressed by a variety of tissues. It is also known as neutral endopeptidase, and enkephalinase. NEP cleaves peptides at the N-terminal side of hydrophobic amino acid residues and is responsible for the degradation and inactivation of a variety of physiological substrates. NEP is a major extracellular amyloid beta-peptide degrading enzyme in the brain and targeting NEP is considered a potential therapeutic strategy for the prevention and treatment of Alzheimer's disease. NEP has also been implicated in the pathogenesis of hypertension, diabetes, and cancer. The SensoLyte® 520 Neprilysin Assay Kit employs a novel internally quenched 5-FAM/QXL® FRET substrate for the detection of neprilysin activity. The enzyme cleaves the FRET substrate into two separate fragments resulting in the release of 5-FAM fluorescence, which can be monitored at excitation /emission= 490/520 nm. The long wavelength fluorescence of 5-FAM is less interfered by the autofluorescence of components in biological samples and test compounds. The assay can detect as low as 0.78 ng/mL of active Neprilysin.
The SensoLyte® Green Pin1 Assay Kit uses a fluorogenic substrate in the cis isoform. Pin1 changes substrate into trans conformation, which is then readily cleaved to generate fluorescent signal which can be monitored at Ex/Em=490/520nm. Increase in fluorescence intensity is directly proportional to the Pin1 activity.
Aß (1-42), a major component of amyloid plaques, accumulates in neurons of Alzheimer’s disease brains. Biochemical analysis of the amyloid peptides isolated from Alzheimer’s disease brain indicates that Aß (1-42) is the principal species associated with senile plaque amyloids, while Aß (1-40) is more abundant in cerebrovascular amyloid deposit.
Aß (1-40) together with Aß (1-42) are two major C-terminal variants of the Aß protein constituting the majority of Aßs. These undergo post-secretory aggregation and deposition in the Alzheimer’s disease brain.
AggreSure™ beta-Amyloid (1-42) peptide is pretreated and tested for aggregation using SensoLyte® ThT Aβ42 Aggregation kit (Cat# 72214). Aggregation Guaranteed!
AggreSure™ beta-Amyloid (1-40) peptide is pretreated and tested for aggregation using SensoLyte® ThT Aβ40 Aggregation kit (Cat# 72213). Aggregation is guaranteed.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (45-73) is a 29-amino acid long peptide derived from the Exon 2/Insert 1 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat or four repeat domains (R1-R4), in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (244-274) is a 31-amino acid long peptide derived from the Repeat 1 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (275-305) is a 31-amino acid long peptide derived from the Repeat 2 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (306-336) is a 31-amino acid long peptide derived from the Repeat 3 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (306-336) is a 31-amino acid long peptide derived from the Repeat 3 domain.
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 45.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 45.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.
Recombinant Human Tau (Tau-441) Protein, GST tagged
100 µg
Anaspec
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 71.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.
Recombinant Human Tau (Tau-441) Protein, GST tagged
50 µg
Anaspec
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 71.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.
Aß (1-42), a major component of amyloid plaques, accumulates in neurons of Alzheimer’s disease brains. Biochemical analysis of the amyloid peptides isolated from Alzheimer’s disease brain indicates that Aß (1-42) is the principal species associated with senile plaque amyloids, while Aß (1-40) is more abundant in cerebrovascular amyloid deposit.
Aß (1-40) together with Aß (1-42) are two major C-terminal variants of the Aß protein constituting the majority of Aßs. These undergo post-secretory aggregation and deposition in the Alzheimer’s disease brain.
AggreSure™ beta-Amyloid (1-42) peptide is pretreated and tested for aggregation using SensoLyte® ThT Aβ42 Aggregation kit (Cat# 72214). Aggregation Guaranteed!
AggreSure™ beta-Amyloid (1-40) peptide is pretreated and tested for aggregation using SensoLyte® ThT Aβ40 Aggregation kit (Cat# 72213). Aggregation is guaranteed.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (45-73) is a 29-amino acid long peptide derived from the Exon 2/Insert 1 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat or four repeat domains (R1-R4), in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (244-274) is a 31-amino acid long peptide derived from the Repeat 1 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (275-305) is a 31-amino acid long peptide derived from the Repeat 2 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (306-336) is a 31-amino acid long peptide derived from the Repeat 3 domain.
TAU proteins belong to the microtubule-associated protein (MAP) family and are involved in the pathogenesis of Alzheimer’s disease. In the human brain, there are six TAU isoforms ranging from 352 to 441 amino acids in length. These isoforms vary at the carboxyl terminal according to the presence of either three repeat (3R) or four repeat (R4) domains, in addition to the presence or absence of one or two insert domains at the amino-terminus (see figure below). Tau Peptide (306-336) is a 31-amino acid long peptide derived from the Repeat 3 domain.
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 45.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 45.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.
Recombinant Human Tau (Tau-441) Protein, GST tagged
Cat No.
AS-55557-100
규격
100 µg
제조사
Anaspec
제품정보
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 71.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.
Recombinant Human Tau (Tau-441) Protein, GST tagged
Cat No.
AS-55557-50
규격
50 µg
제조사
Anaspec
제품정보
Microtubule associated protein (Tau) is found predominantly in the central neural system and its major function is to promote assembly and to stabilize neuronal microtubules. Six isoforms of Tau were identified in humans that are differentiated by the exclusion or inclusion of exons 2, 3, and 10. Tau-441 is the longest of Tau isoforms, consisting of 441 amino acids with molecular mass of 71.8 kDa. Under physiological conditions Tau can undergo abnormal phosphorylation, truncation, or other modifications that result in the protein detachment from microtubules. These modified Tau molecules can self-associate and form different types of aggregates including neurofibrillary tangles (NFTs) found in brains of patients with neurodegenerative diseases such as Alzheimer’s disease.