Molecular Mechanisms, Biomarker Value, and Advances in Targeted Therapy for Core Pathological Targets in Alzheimer’s Disease
Molecular Mechanisms, Biomarker Value, and Advances in Targeted Therapy for Core Pathological Targets in Alzheimer’s Disease
Alzheimer’s disease is jointly driven by Aβ deposition, Tau abnormalities, neuroinflammation, disrupted lipid metabolism, and synaptic injury. Defining the core targets at different pathological stages provides the basis for disease stratification, therapeutic monitoring, and the design of combination treatments.
Keywords: Alzheimer’s disease; Aβ; Tau; BACE1; ApoE; neuroinflammation; neurotrophic factor; biomarker; GLP-1R; targeted therapy
1 Pathological Characteristics and Target Systems of Alzheimer’s Disease
1.1 Aβ Plaques and Tau Neurofibrillary Tangles
The main pathological characteristics of Alzheimer’s disease include extracellular Aβ deposition, aggregation of abnormally phosphorylated Tau within neurons, synaptic loss, and progressive neuronal death. Aβ abnormalities generally appear relatively early and can promote Tau phosphorylation, glial cell activation, and neural network dysfunction. The regional spread of Tau pathology is more closely associated with neurodegeneration and cognitive decline.
1.2 Temporal Sequence of Pathological Processes
Aβ accumulation may begin many years before obvious cognitive symptoms appear, followed by increases in soluble phosphorylated Tau, Tau aggregation, neuroinflammation, synaptic injury, and brain atrophy. These processes are not connected in a simple linear sequence but amplify one another through networks involving Aβ-Tau, Tau-inflammation, ApoE-microglia, and vascular-neuronal interactions.
Figure 1. Multiple pathogenic mechanisms of Alzheimer’s disease leading to neuronal injury, synaptic dysfunction, and cognitive decline
1.3 Core Targets and Regulatory Targets
APP, BACE1, γ-secretase, Aβ, and Tau are core targets that directly determine the formation of characteristic pathology. ApoE, TREM2, NLRP3, complement, oxidative stress, and neurotrophic factors regulate pathological protein clearance, inflammatory responses, and neuronal vulnerability. Targeting core pathology can reduce pathological burden, whereas targeting regulatory networks is more suitable for protecting synapses, improving the microenvironment, and delaying secondary injury.
1.4 Pathological Heterogeneity of Alzheimer’s Disease
Patients may simultaneously exhibit cerebrovascular lesions, α-synuclein deposition, TDP-43 abnormalities, and other age-related pathologies. Therefore, the same Aβ or Tau burden does not necessarily produce the same cognitive manifestations. Disease evaluation should use core Aβ and Tau biomarkers to determine the biological state of Alzheimer’s disease and should integrate neurodegenerative, inflammatory, and copathological indicators to interpret disease stage and individual variation.
Table 1 Major Pathological Targets in Alzheimer’s Disease and Their Research Positioning
Target System | Representative Molecules | Main Pathological Roles | Major Evaluation Indicators |
Aβ production | APP, BACE1, γ-secretase | Produces Aβ40 and Aβ42 | Aβ42, Aβ40, sAPPβ, and β-CTF |
Aβ aggregation and clearance | Aβ oligomers, LRP1, ApoE, TREM2 | Regulates oligomerization, plaque formation, and cerebral clearance | Aβ42/40 and amyloid PET |
Tau abnormalities | GSK-3β, CDK5, PP2A, Tau | Promotes Tau phosphorylation, aggregation, and propagation | p-Tau181, p-Tau217, and Tau PET |
Neuroinflammation | TREM2, NLRP3, C1q, C3 | Regulates microglial activation and synaptic phagocytosis | GFAP, sTREM2, and inflammatory factors |
Oxidative injury and cell death | ROS, mitochondria, Caspases, ferroptosis pathways | Promotes neuronal dysfunction and death | 4-HNE, 8-OHdG, and Caspase-3 |
Lipid metabolism | ApoE, ABCA1, LDLR, LRP1 | Influences lipid transport, Aβ clearance, and inflammation | APOE genotype and ApoE protein |
Synaptic protection | BDNF, NGF, TrkB, TrkA | Maintains plasticity and cholinergic neurons | BDNF, Synaptophysin, and PSD-95 |
2 Targets Related to Aβ Production, Aggregation, and Clearance
2.1 Two APP Processing Pathways
APP can be cleaved by α-secretase through the non-amyloidogenic pathway, producing soluble sAPPα and preventing formation of the complete Aβ sequence. Alternatively, APP can first be cleaved by BACE1 to generate sAPPβ and β-CTF, followed by γ-secretase cleavage to produce Aβ peptides of different lengths. Aβ42 is relatively hydrophobic and has a strong tendency to aggregate, making it an important component of amyloid plaques and toxic oligomers.
2.2 BACE1 and the Initial Step of Aβ Production
BACE1 mediates the initial cleavage of the amyloidogenic pathway and is a direct target for reducing Aβ production. BACE1 inhibition decreases the formation of β-CTF and Aβ. However, BACE1 also processes substrates associated with axonal guidance, myelination, and synaptic function. High-intensity, long-term inhibition may therefore interfere with normal neural function.
2.3 The γ-Secretase Complex
The γ-secretase complex consists of Presenilin, Nicastrin, APH-1, PEN-2, and other components. It cleaves APP and influences the carboxyl-terminal length of Aβ. Presenilin mutations can alter the ratio of Aβ42 to shorter Aβ peptides. However, γ-secretase also participates in the processing of Notch and many other proteins, and complete direct inhibition can interfere with normal cell differentiation and signal transduction.
2.4 Formation of Aβ Oligomers and Fibrils
Aβ monomers can form oligomers, protofibrils, and mature fibrils. Soluble Aβ oligomers disrupt NMDA receptors, calcium homeostasis, mitochondria, and synaptic plasticity, and their neurotoxicity does not depend entirely on total plaque burden. Aβ studies must therefore distinguish among monomers, oligomers, fibrils, and plaques rather than using total Aβ changes alone to determine whether toxicity has been reduced.
2.5 Cellular and Vascular Clearance of Aβ
Aβ can be phagocytosed by microglia and astrocytes, removed through cerebrospinal fluid and the glymphatic pathway, and transported across the blood-brain barrier through systems such as LRP1. ApoE lipidation status, TREM2 function, blood-brain barrier integrity, and cerebrospinal fluid flow all affect clearance efficiency. Impaired clearance is an important cause of Aβ accumulation in sporadic Alzheimer’s disease.
2.6 Cerebral Amyloid Angiopathy
Aβ can deposit in cerebral vessel walls and form cerebral amyloid angiopathy, disrupting vascular integrity and increasing the risk of microhemorrhage. Mobilization of parenchymal and vascular Aβ during anti-Aβ treatment may cause cerebral edema or microhemorrhage. Treatment risk should therefore be evaluated using MRI, APOE genotype, and assessment of cerebrovascular lesions.
3 Abnormal Tau Phosphorylation and Neurofibrillary Tangle Formation
3.1 Normal Physiological Functions of Tau
Tau is mainly distributed in neuronal axons and maintains microtubule stability, axonal structure, and intracellular transport by binding to microtubules. Tau-microtubule binding is dynamically regulated by phosphorylation. Moderate phosphorylation facilitates cytoskeletal remodeling, whereas sustained hyperphosphorylation reduces the affinity of Tau for microtubules.
3.2 Imbalance Between Tau Kinases and Phosphatases
Kinases such as GSK-3β, CDK5, and MAPK can phosphorylate Tau, whereas PP2A is the principal phosphatase responsible for Tau dephosphorylation. Aβ, inflammation, calcium imbalance, and oxidative stress can enhance Tau kinase activity or reduce PP2A function, causing abnormal phosphorylation at sites including Thr181, Thr217, Thr231, Ser202, and Thr205.
3.3 Tau Aggregation and Tangle Formation
Tau released from microtubules can undergo conformational changes, truncation, and abnormal modifications, followed by formation of oligomers, paired helical filaments, and neurofibrillary tangles. Tau oligomers can impair mitochondria, protein degradation systems, and synaptic function, whereas mature tangles reflect the sustained accumulation of Tau pathology.
3.4 Propagation of Tau Through Neural Networks
Pathological Tau can be released from neurons, taken up by neighboring or synaptically connected neurons, and induce misfolding of endogenous Tau. Abnormal Tau can spread along neural connections from the entorhinal cortex to the hippocampus and related cortical regions. Therefore, blocking Tau seed formation, extracellular release, or cellular uptake may have therapeutic value.
3.5 Synergy Between Aβ and Tau
Aβ can promote Tau phosphorylation and propagation by activating GSK-3β, inflammatory pathways, and neuronal hyperexcitability. Tau participates in mediating Aβ-induced axonal, synaptic, and neural network injury. Reducing Aβ is more suitable for early disease stages, whereas directly inhibiting Tau aggregation and propagation may remain valuable after Tau pathology has already developed.
4 Targets Related to Neuroinflammation, Oxidative Stress, and Neuronal Apoptosis
4.1 TREM2 and Microglial Responses
TREM2 participates in microglial recognition of lipids, dead cells, and Aβ deposits and regulates migration, phagocytosis, and metabolic adaptation. Impaired TREM2 function alters the microglial barrier around plaques and Aβ clearance. However, excessively or persistently activated microglia can also release inflammatory mediators. The intervention objective should therefore be to restore an effective clearance response rather than completely suppress microglia.
4.2 NLRP3 Inflammasome
Aβ oligomers, Tau aggregates, mitochondrial ROS, and lysosomal injury can activate the NLRP3 inflammasome in microglia, promoting Caspase-1 activation and maturation of IL-1β and IL-18. Inhibition of NLRP3 or Caspase-1 can reduce inflammatory signaling and may improve Aβ clearance and Tau abnormalities.
4.3 Astrocytes and the Complement Pathway
Reactive astrocytes can alter glutamate uptake, cholesterol supply, blood-brain barrier support, and inflammatory factor secretion. Aβ can also induce deposition of complement components such as C1q and C3 near synapses, causing microglia to recognize and engulf synapses through complement receptors and leading to early synaptic loss.
4.4 Mitochondrial Function and Oxidative Stress
Both Aβ and abnormal Tau can impair the mitochondrial respiratory chain, mitochondrial dynamics, and axonal transport, increasing ROS production and reducing ATP generation. ROS further oxidizes lipids, proteins, and DNA and promotes BACE1 expression, abnormal Tau modification, and inflammasome activation, forming a cycle in which oxidative injury and pathological proteins amplify one another.
4.5 Neuronal Apoptosis and Other Forms of Cell Death
Sustained calcium overload, loss of mitochondrial membrane potential, and cytochrome c release can activate Caspase-9- and Caspase-3-mediated apoptosis. Lipid peroxidation, glutathione depletion, and iron homeostasis abnormalities may promote ferroptosis, whereas NLRP3- and Gasdermin-associated signaling can induce inflammatory cell death. Multiple forms of cell death may coexist, and detection of Caspase-3 alone is insufficient to fully characterize neuronal injury.
5 ApoE and Lipid Metabolism-Mediated Genetic Risk of Alzheimer’s Disease
5.1 ApoE Isoforms and Genetic Risk
Human ApoE has three major isoforms: ApoE2, ApoE3, and ApoE4. APOE ε4 is an important common genetic risk factor for late-onset Alzheimer’s disease and can increase disease probability and advance the onset of pathology. APOE ε2 generally has a partially protective effect, although the actual risk is also influenced by age, sex, and other genetic backgrounds.
5.2 Effects of ApoE on Aβ Aggregation and Clearance
ApoE can bind Aβ and influence its aggregation, cellular uptake, and transport across the blood-brain barrier. ApoE4-associated Aβ complexes are cleared less efficiently and may promote Aβ accumulation in the brain parenchyma and blood vessels. ApoE2 and ApoE3 are generally more favorable for Aβ transport and clearance.
5.3 ApoE Lipidation and Cholesterol Transport
ApoE is mainly produced by astrocytes and activated microglia and transports cholesterol and phospholipids to neurons after ABCA1-mediated lipidation. Insufficient lipidation of ApoE4 alters membrane lipid composition, synaptic repair, endosomal transport, and receptor recycling, increasing neuronal vulnerability to metabolic and proteostasis stress.
5.4 ApoE and TREM2-Dependent Microglial States
ApoE and TREM2 jointly regulate the transcriptional state, migration, and phagocytic function of plaque-responsive microglia. Different APOE and TREM2 risk variants can alter microglial aggregation around, encapsulation of, and clearance responses to Aβ. ApoE-targeted therapy may therefore affect lipid transport, inflammatory states, and Aβ processing simultaneously.
5.5 Directions for ApoE-Targeted Intervention
ApoE-related strategies include reducing harmful ApoE4 levels, enhancing ApoE lipidation, correcting ApoE4 conformation, promoting conversion of ApoE4 toward ApoE3-like function, and regulating ApoE receptors and the TREM2 pathway. Because ApoE performs normal lipid transport functions, complete ApoE elimination may create new neurological metabolic problems.
6 Neurotrophic Factors and Mechanisms of Synaptic Protection
6.1 BDNF-TrkB Signaling
BDNF binding to TrkB activates the PI3K/AKT, MAPK/ERK, and PLCγ pathways and promotes neuronal survival, dendritic spine formation, and long-term potentiation. Aβ, Tau, and chronic inflammation can reduce BDNF expression or weaken TrkB signaling, impairing hippocampal synaptic plasticity. Restoring BDNF-TrkB function may provide a neuroprotective strategy in addition to pathological protein clearance.
6.2 NGF-TrkA and Cholinergic Neurons
NGF regulates the survival, axonal projection, and cholinergic function of basal forebrain cholinergic neurons through TrkA and p75NTR. Loss of basal forebrain cholinergic neurons and reduced TrkA signaling in Alzheimer’s disease are associated with impaired attention, learning, and memory. However, the limited ability of NGF to cross the blood-brain barrier restricts systemic administration.
6.3 Presynaptic and Postsynaptic Dysfunction
Aβ oligomers inhibit synaptic transmission and long-term potentiation, whereas abnormal Tau impairs axonal transport, synaptic vesicles, and the dendritic spine cytoskeleton. Synaptophysin, Synapsin, PSD-95, Homer1, and dendritic spine density can be used to evaluate synaptic structures. Electrophysiological long-term potentiation and neural network activity reflect functional changes.
6.4 Imbalance in Neuronal Excitability
Neuronal hyperexcitability and abnormal network synchronization may occur during early disease stages and subsequently progress to synaptic failure. Aβ can impair glutamate clearance and alter NMDA receptor regulation, whereas Tau can affect axonal and inhibitory neural network function. The goal of synaptic protection is to restore the balance between excitation and inhibition rather than simply increase neural activity.
7 Detection of Alzheimer’s Disease Biomarkers and Disease Stratification
7.1 Cerebrospinal Fluid Aβ42/40
Reduced cerebrospinal fluid Aβ42 reflects deposition of Aβ in the brain. The Aβ42/40 ratio can reduce the effects of individual variation in total Aβ production and preanalytical factors. This ratio can be used to identify amyloid pathology but does not directly evaluate the extent of neuronal injury.
7.2 Phosphorylated Tau and Total Tau
Cerebrospinal fluid and plasma p-Tau181, p-Tau217, and p-Tau231 reflect Aβ-associated Tau abnormalities. Total Tau more closely reflects neuronal injury and protein release and is less disease-specific than phosphorylated Tau. The two types of markers cannot substitute for one another.
7.3 Plasma p-Tau217
Plasma p-Tau217 has a high capacity to distinguish Alzheimer’s disease-associated Aβ and Tau pathology and can be used for preliminary screening and disease stratification, reducing the need for cerebrospinal fluid testing or PET scans in some populations. Clinical application requires validated assay platforms, thresholds, and stratified interpretation procedures.
7.4 GFAP, NfL, and sTREM2
Plasma or cerebrospinal fluid GFAP reflects astrocytic responses, neurofilament light chain (NfL) reflects axonal injury, and sTREM2 can be used to evaluate microglia-associated responses. These indicators are not specific to Alzheimer’s disease but can be used to assess neuroinflammation, the degree of neurodegeneration, and non-Aβ effects after treatment.
7.5 Amyloid PET and Tau PET
Amyloid PET displays cerebral Aβ burden and can be used to confirm eligibility for anti-Aβ treatment. Tau PET more closely reflects the regional spread of Tau pathology and clinical severity. PET quantification can support disease stratification and therapeutic monitoring but is limited by tracer characteristics, thresholds, cost, and accessibility.
7.6 MRI and Evaluation of Neurodegeneration
Structural MRI can assess atrophy of the hippocampus, entorhinal cortex, and whole brain and can identify microhemorrhage, cortical superficial siderosis, and cerebrovascular lesions. Diffusion imaging, functional MRI, and cerebral perfusion indicators can supplement information on neural networks and white matter injury, but these changes are not specific to Alzheimer’s disease.
7.7 Biological Diagnosis and Clinical Staging
Alzheimer’s disease stratification should use core Aβ and Tau biomarkers to determine biological status and should integrate cognitive function, activities of daily living, neurodegeneration, and copathological indicators for clinical staging. Abnormal biomarkers in asymptomatic individuals do not mean that dementia will inevitably develop in the short term. Age, pathological burden, and coexisting diseases must also be considered.
Table 2 Interpretive Value of Major Alzheimer’s Disease Biomarkers
Biomarker | Major Sample or Technology | Main Significance | Major Limitations |
Aβ42/40 | Cerebrospinal fluid and plasma | Reflects amyloid pathology | Limited reflection of the degree of neurodegeneration |
p-Tau181 | Cerebrospinal fluid and plasma | Reflects Aβ-associated Tau abnormalities | Early sensitivity may be lower than that of p-Tau217 |
p-Tau217 | Cerebrospinal fluid and plasma | Identifies Alzheimer’s disease pathology and supports stratification | Thresholds require independent validation for different platforms |
Total Tau | Cerebrospinal fluid | Reflects neuronal injury | Insufficient disease specificity |
GFAP | Plasma and cerebrospinal fluid | Reflects astrocytic responses | Can be elevated in multiple brain diseases |
NfL | Plasma and cerebrospinal fluid | Reflects axonal injury | Cannot determine the cause of injury |
Amyloid PET | PET | Displays Aβ deposition | Does not directly evaluate neuronal function |
Tau PET | PET | Displays regional Tau burden | Interpretation is influenced by tracer and disease stage |
MRI | Structural and vascular imaging | Evaluates atrophy, microhemorrhage, and copathology | Lacks Alzheimer’s disease specificity |
8 Aβ-, Tau-, BACE1-, and GLP-1R-Targeted Therapeutic Strategies
8.1 Aβ Monoclonal Antibodies
Anti-Aβ monoclonal antibodies recognize soluble aggregates, protofibrils, or plaque-associated Aβ, promote immune clearance, and reduce cerebral amyloid burden. Representative drugs include Lecanemab and Donanemab. Their principal role is to slow clinical decline in early Alzheimer’s disease rather than restore neurons that have already been lost. Aβ pathology must be confirmed before treatment, and amyloid-related imaging abnormalities such as cerebral edema and microhemorrhage must be monitored.
8.2 Tau-Targeted Therapy
Tau therapeutic strategies include inhibiting Tau kinases, enhancing PP2A activity, blocking Tau aggregation, promoting intracellular Tau degradation, and using antibodies to neutralize extracellular Tau seeds. Major challenges include limited antibody entry into neurons, complex Tau epitopes and conformations, differences among stages of pathological propagation, and treatment initiation after pathology has become advanced.
8.3 BACE1 Inhibition
BACE1 inhibitors can substantially reduce Aβ production, but high-intensity, long-term inhibition has not consistently improved cognition, and some candidates have caused cognitive, neuropsychiatric, or hepatic safety problems. Subsequent research has placed greater emphasis on earlier intervention, lower inhibition intensity, and increased selectivity for pathological APP processing.
8.4 GLP-1R-Targeted Strategies
GLP-1R activation can regulate insulin signaling, mitochondrial function, neuroinflammation, and cell survival and has therefore been investigated as a metabolic intervention for Alzheimer’s disease. Current evidence is insufficient to establish GLP-1R agonists as confirmed disease-modifying treatments for Alzheimer’s disease. Their main research value lies in examining the relationships among metabolic abnormalities, inflammation, and neuroprotection.
8.5 Patient Selection for Targeted Therapy
Anti-Aβ treatment requires confirmation of cerebral Aβ pathology and patient selection based on disease stage, MRI findings, APOE ε4 status, and cerebrovascular risk. Tau-, inflammation-, and neuroprotection-directed treatments should be stratified according to Tau burden, glial biomarkers, the degree of neurodegeneration, and copathological status rather than using the same target for all patients.
8.6 Directions for Combination Therapy
Alzheimer’s disease treatment may require reducing Aβ production or deposition during early stages, limiting Tau propagation and neuroinflammation during pathological expansion, and continuously protecting synaptic, mitochondrial, and cerebrovascular function. Combination regimens must define the pathological stage and biomarker endpoint corresponding to each drug. Simply combining multiple targets does not guarantee synergy.
Table 3 Major Targeted Therapeutic Strategies for Alzheimer’s Disease
Therapeutic Direction | Main Targets | Major Actions | Key Limitations |
Anti-Aβ antibodies | Aβ protofibrils, aggregates, or plaques | Reduce amyloid burden and slow early clinical decline | ARIA, infusion burden, and patient selection |
Tau immunotherapy | Extracellular Tau seeds | Limits Tau propagation | Limited coverage of intracellular pathology |
Tau kinase inhibition | GSK-3β and CDK5 | Reduces abnormal Tau phosphorylation | Kinases have broad physiological substrates |
BACE1 inhibition | BACE1 | Reduces Aβ production | High-intensity inhibition may impair normal neural function |
Neuroinflammation regulation | TREM2, NLRP3, and complement | Improves clearance responses and reduces synaptic injury | Inflammation has stage-dependent and dual effects |
ApoE regulation | ApoE4, ABCA1, and LRP1 | Improves lipid transport and Aβ clearance | Normal lipid functions cannot be completely suppressed |
GLP-1R activation | GLP-1R | Regulates metabolism, inflammation, and cell-survival signaling | Clinical disease-modifying effects have not been established |
Neurotrophic support | BDNF-TrkB and NGF-TrkA | Protects synapses and cholinergic neurons | Difficulties in blood-brain barrier penetration and target-region delivery |
9 Products Related to Core Alzheimer’s Disease Pathology and Biomarker Research
9.1 Core Proteins, Antibodies, and Detection Reagents
Catalog # | Product Name | Grade & Purity | Main Application |
Amyloid β Protein Fragment 1-42， TFA | ≥95% | Preparation of Aβ42 monomers, oligomers, and fibrils and establishment of aggregation and neurotoxicity models | |
β-Amyloid (1-40) (TFA) | ≥95% | Studies of Aβ40 aggregation, vascular deposition, and differences from Aβ42 | |
β Amyloid (1-42) (scrambled) | — | Scrambled peptide control for Aβ42 aggregation and neurotoxicity experiments | |
Biotinyl-Ahx-Amyloid β-Protein (1-42) | — | Aβ42 binding, capture, and antibody-recognition studies | |
FITC-β-Ala-Amyloid β-Protein (1-42) | — | Tracking of Aβ42 uptake, cellular localization, and clearance | |
Lecanemab (anti-Amyloid Beta) | Animal Free, carrier-free, recombinant, ExactAb™, low endotoxin, azide-free, validated, ≥95% (SDS-PAGE & SEC-HPLC), see COA | Studies of Aβ aggregate recognition, antibody binding, and immune clearance | |
Donanemab (anti-Amyloid Beta) | Animal Free, carrier-free, recombinant, ExactAb™, low endotoxin, azide-free, validated, ≥95% (SDS-PAGE & SEC-HPLC), see COA | Studies of plaque-associated Aβ recognition and antibody-mediated clearance | |
Crenezumab (anti-Amyloid Beta) | Animal Free, carrier-free, recombinant, ExactAb™, low endotoxin, azide-free, validated, ≥95% (SDS-PAGE & SEC-HPLC), see COA | Comparison of the binding and clearance characteristics of different anti-Aβ antibodies | |
Recombinant Human Amyloid Precursor Protein | Animal Free, carrier-free, bioactive, ActiBioPure™, azide-free, His Tag, ≥95% (SDS-PAGE) | APP processing, protein interaction, and secretase-cleavage studies | |
Recombinant Amyloid Precursor Protein Antibody | Recombinant, ExactAb™, validated, 0.4 mg/mL | Detection of APP expression and intracellular localization | |
Human Amyloid Precursor Protein (APP) ELISA Kit | BioReagent | Quantitative detection of APP levels in human samples | |
Recombinant human BACE1 protein | Animal Free, carrier-free, bioactive, ActiBioPure™, azide-free, His Tag, ≥90% (SDS-PAGE) | BACE1 activity assays and inhibitor screening | |
MCA-EIDLMVLDK-Dnp, TFA salt | ≥98% | Fluorescence-based measurement of BACE1 cleavage activity | |
BACE1 Mouse mAb | Carrier-free, ExactAb™, validated, see COA | Detection of BACE1 expression and changes in the APP amyloidogenic processing pathway | |
BACE1 Human Pre-designed siRNA Set A | — | BACE1 knockdown and validation of BACE1-dependent Aβ production | |
Recombinant Human Tau Protein | Animal Free, carrier-free, bioactive, ActiBioPure™, His Tag, ≥95% (SDS-PAGE) | Tau phosphorylation, aggregation, and antibody-binding studies | |
APOE Human Pre-designed siRNA Set A | — | APOE knockdown and studies of lipid transport, Aβ clearance, and glial responses | |
pLenti-APOE-sgRNA | — | Negative control for ApoE protein detection and antibody-specificity validation | |
Recombinant Mouse APOE Protein | ≥90% (SDS-PAGE) | ApoE lipid metabolism, receptor binding, and Aβ interaction studies | |
Human APOE ELISA Kit | Bioactive, for Enzyme immunoassay(ELISA), for ELISA | Quantitative detection of ApoE levels in human samples | |
PY314 (anti-TREM2) | Animal Free, carrier-free, recombinant, ExactAb™, low endotoxin, azide-free, validated, ≥95% (SDS-PAGE & SEC-HPLC), see COA | TREM2 antibody binding and regulation of microglial signaling | |
TREM2 Human Pre-designed siRNA Set A | — | TREM2 knockdown and studies of microglial phagocytosis and inflammatory responses | |
Mouse Triggering Receptor Expressed On Myeloid Cells 2 (TREM2) ELISA Kit | BioReagent | Quantitative detection of TREM2 in mouse samples | |
Recombinant Human BDNF GMP Protein | Animal Free, carrier-free, bioactive, ActiBioPure™, high-performance, sterile, ≥70% (SDS-PAGE) | BDNF-TrkB signaling, neuronal survival, and synaptic protection studies | |
BDNF Antibody | ExactAb™, validated, 1.0 mg/mL | Detection of BDNF expression and changes in neurotrophic signaling | |
Human pro-Brain Derived Neurotrophic Factor (proBDNF) ELISA Kit | BioReagent | Quantitative detection of ProBDNF and evaluation of precursor-processing changes | |
Human Mature Brain-derived Neurotrophic Factor(mBDNF) ELISA Kit | BioReagent | Quantitative detection of mature BDNF levels | |
Human Brain Derived Neurotrophic Factor (BDNF) ELISA Kit | BioReagent | Detection of total BDNF levels in human samples | |
Recombinant Human beta-NGF Protein | Animal Free, carrier-free, bioactive, ActiBioPure™, high-performance, PBS Only, ≥90% (SDS-PAGE & SEC-HPLC) | NGF-TrkA signaling, cholinergic neuronal survival, and axonal growth studies | |
Recombinant Human NGFR/TNFRSF16 Protein | Animal Free, carrier-free, bioactive, ActiBioPure™, high-performance, His Tag, Fc tag, ≥95% (SDS-PAGE) | NGF-p75NTR binding and receptor-signaling studies | |
NGF Mouse mAb | Carrier-free, ExactAb™, azide-free, validated, high-performance, see COA | Detection of NGF expression and changes in neurotrophic signaling | |
Recombinant NGFR Antibody | Recombinant, ExactAb™, validated, 2.0 mg/mL | Detection of p75NTR/NGFR expression and receptor-level changes | |
Human Nerve Growth Factor (NGF) ELISA Kit | BioReagent | Quantitative detection of NGF in human samples | |
Recombinant Human NLRP3 Protein | Carrier-free, His Tag, ≥90% (SDS-PAGE) | NLRP3 protein-interaction, antibody-screening, and inflammasome studies | |
NLRP3 Human Pre-designed siRNA Set A | — | NLRP3 knockdown and validation of inflammasome-dependent responses | |
Human NLR Family, Pyrin Domain Containing Protein 3 (NALP3/NLRP3) ELISA Kit | BioReagent | Quantitative detection of NLRP3 in human samples | |
Iba1 Mouse mAb | Animal Free, carrier-free, ExactAb™, azide-free, validated, high-performance, PBS Only, ≥95% (SDS-PAGE), 1.0 mg/mL | Detection of microglia and their activation status | |
GFAP Antibody | Carrier-free, ExactAb™, azide-free, validated, high-performance, see COA | Detection of astrocytic responses | |
Human Glial Fibrillary Acidic Protein (GFAP) ELISA Kit | BioReagent | Quantitative evaluation of astrocytic responses in human samples | |
Recombinant Synaptophysin Antibody | Recombinant, ExactAb™, validated, 0.48 mg/mL | Detection of presynaptic structures and synaptic loss | |
Recombinant PSD95 Antibody | Recombinant, ExactAb™, validated, high-performance, see COA | Detection of the postsynaptic density and synaptic integrity | |
Human Beta Amyloid 40 (Aβ40) ELISA Kit | BioReagent | Quantitative detection of Aβ40 and calculation of the Aβ42/40 ratio | |
Human Beta Amyloid 42 (Aβ42) ELISA Kit | BioReagent | Quantitative detection of Aβ42 and changes in amyloid pathology | |
Human Phosphorylated Tau181 Protein (p-TAU181) ELISA Kit | BioReagent | Quantitative detection of p-Tau181 | |
Human Phosphorylated Tau-217 Protein(p-Tau217) ELISA Kit | BioReagent | Quantitative detection of p-Tau217 and support for Alzheimer’s disease stratification | |
Human Phosphorylated Tau231 Protein (231P-tau) ELISA Kit | BioReagent | Quantitative detection of p-Tau231 and early Tau abnormalities | |
Human Neurofilament Light Chain (NFL) ELISA Kit | BioReagent | Quantitative evaluation of axonal injury and neurodegenerative changes |
Alzheimer’s disease cannot be fully explained by a single pathological process. Aβ is suitable for early pathological confirmation and intervention against amyloid burden, whereas Tau more closely reflects disease spread and the progression of neurodegeneration. ApoE, neuroinflammation, and neurotrophic pathways determine pathological clearance, synaptic vulnerability, and treatment responses. Identifying the pathological stage using biomarkers and selecting corresponding targets are essential for improving the effectiveness of disease-modifying therapy.
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