Technical Routes and Result Interpretation in Cell Autophagy Detection
Technical Routes and Result Interpretation in Cell Autophagy Detection
Cell autophagy is an important homeostatic regulatory process in which cells degrade cytoplasmic proteins, damaged organelles, protein aggregates, and some exogenous components through the lysosomal system. The core of autophagy detection is not merely observing autophagosome number or changes in a single marker protein, but determining whether autophagic flux is complete, namely whether autophagosome formation, maturation, fusion with lysosomes, and substrate degradation proceed continuously.
Keywords: cell autophagy; autophagic flux; LC3; p62/SQSTM1; Beclin 1; ATG proteins; autophagosome; autolysosome; lysosomal function; Western blot; fluorescence imaging; transmission electron microscopy; mitophagy
1、Basic Principles of Cell Autophagy Detection
1.1 Detection Nodes in the Autophagy Process
(1) Autophagy initiation
Autophagy initiation is usually associated with nutrient deprivation, energy stress, oxidative stress, endoplasmic reticulum stress, drug stimulation, or organelle damage. The ULK1 complex, Beclin 1, VPS34 complex, and ATG proteins participate in autophagic membrane nucleation and elongation. Detection at this stage may include Beclin 1, ATG5, ATG7, ULK1 phosphorylation, and changes in mTOR/AMPK signaling. However, these indicators can only suggest the regulatory status of autophagy and cannot independently prove enhanced autophagic flux.
(2) Autophagosome formation
During autophagosome formation, LC3-I undergoes lipidation to form membrane-bound LC3-II, which localizes to the autophagosomal membrane. Increased LC3-II, increased LC3 puncta, or elevated autophagosome numbers may all indicate increased autophagosome formation. However, an increase in autophagosomes may result either from enhanced autophagy induction or from impaired autophagosome degradation, so flux experiments are required for interpretation.
(3) Autophagosome maturation and lysosomal fusion
Mature autophagosomes fuse with lysosomes to form autolysosomes, where substrates are degraded in an acidic environment by lysosomal hydrolases. If lysosomal acidification, membrane fusion, or protease activity is impaired, LC3-II and p62 may accumulate. In this case, the apparent increase in autophagy-related structures may actually reflect blockade at the degradation stage of autophagy.
(4) Substrate degradation
Selective autophagy receptors such as p62/SQSTM1 and NBR1 bind ubiquitinated substrates and interact with LC3, after which they enter lysosomes for degradation during autophagy. A decrease in p62 usually suggests enhanced autophagic substrate degradation, whereas p62 accumulation suggests insufficient substrate clearance or autophagy blockade. However, p62 is also regulated by transcription, oxidative stress, and inflammatory signaling, and should not be used as the only criterion.
1.2 Core Logic of Autophagy Detection
(1) Distinguishing autophagosome number from autophagic flux
Increased LC3-II, increased autophagosomes, and increased LC3 fluorescent puncta are all autophagy-related phenotypes, but they do not directly equal enhanced autophagy. Autophagic flux emphasizes the dynamic process and requires comparison of LC3-II, p62, and autophagy reporter signals before and after lysosomal blockade.
(2) Combining structural, protein, and functional indicators
Reliable autophagy detection generally requires at least three levels of evidence: LC3-II or LC3 puncta to reflect autophagosome formation, p62/NBR1 to reflect substrate degradation, and Bafilomycin A1, chloroquine, or dual-fluorescence LC3 systems to reflect flux status. A single indicator is suitable only as suggestive evidence.
(3) Simultaneously evaluating cellular status
Cell death, protein synthesis inhibition, lysosomal damage, mitochondrial depolarization, and cell cycle changes can all affect autophagy detection results. Autophagy experiments should simultaneously evaluate cell viability, apoptosis/necrosis, lysosomal acidification, total protein degradation, and treatment-dose toxicity.
Table 1 Core Indicators and Interpretation Boundaries in Cell Autophagy Detection
Detection level | Common indicators | What it can indicate | Interpretation limitations |
Autophagy initiation | ULK1, Beclin 1, VPS34, ATG proteins | Whether autophagy regulatory pathways are activated or inhibited | Cannot directly indicate flux changes |
Autophagosome formation | LC3-II, LC3 puncta, autophagosome number | Changes in autophagosome formation or LC3 lipidation | Cannot distinguish increased formation from impaired degradation |
Autophagic substrate degradation | p62/SQSTM1, NBR1, ubiquitinated proteins | Whether substrates accumulate or are cleared | Affected by transcription, protein synthesis, and proteasome activity |
Autophagic flux | LC3-II changes before and after lysosomal inhibitors | Dynamic status of autophagosome formation and degradation | Requires optimization of inhibitor concentration and treatment time |
Lysosomal function | LAMP1, LAMP2, LysoTracker, cathepsin activity | Lysosomal acidification, fusion, and degradation capacity | Cannot independently represent autophagy initiation |
Ultrastructure | Autophagosomes and autolysosomes under TEM | Presence of autophagy-related membranous structures | Limited ability to determine flux |
2、LC3-Related Detection Methods
2.1 LC3-I/LC3-II Western Blot
(1) Detection principle
LC3 is the most commonly used marker protein in cell autophagy detection. Cytosolic LC3-I is lipidated to form LC3-II, which localizes to the autophagosomal membrane. Western blot usually detects the conversion from LC3-I to LC3-II and uses LC3-II relative to an internal control or the LC3-II/LC3-I ratio as a reference indicator for autophagosome formation.
(2) Result interpretation
Increased LC3-II suggests an increase in autophagy-related membrane structures, but the reason may be enhanced autophagy induction or impaired autophagosome-lysosome fusion or degradation. If LC3-II further accumulates after adding Bafilomycin A1 or chloroquine, this indicates that autophagosomes are still being continuously formed and entering the degradation pathway. If LC3-II does not increase further after blockade, insufficient autophagosome generation or pre-existing flux obstruction should be considered.
(3) Technical points
LC3-II has a small molecular weight and is sensitive to gel concentration, transfer efficiency, and antibody specificity. Lysis conditions must sufficiently extract membrane-bound LC3-II to avoid signal underestimation caused by incomplete lysis. Basal LC3 levels differ greatly among cell types, so absolute grayscale values should not be directly compared across cell lines.
2.2 LC3 Immunofluorescence and Puncta Analysis
(1) Detection principle
Under basal conditions, LC3 usually shows diffuse distribution. When autophagosome formation increases, LC3 may form punctate aggregates. LC3 immunofluorescence or a GFP-LC3 expression system can be used to observe the number, area, and spatial distribution of intracellular LC3 puncta.
(2) Result interpretation
Increased LC3 puncta suggest an increase in autophagosomes or LC3-positive membrane structures, but this alone cannot prove enhanced autophagic flux. If increased LC3 puncta are accompanied by p62 reduction and lysosomal inhibitors can further increase LC3 puncta, enhanced autophagic flux is more strongly supported. If increased LC3 puncta are accompanied by p62 accumulation, blockade at the autophagic degradation stage is more likely.
(3) Technical points
GFP-LC3 overexpression may form nonspecific protein aggregates and generate false-positive puncta. Transfection amount and expression level should be controlled, and empty vector, positive induction, lysosomal blockade, and untreated controls should be included. Image quantification should calculate puncta number per cell, puncta area, proportion of positive cells, or fluorescence intensity distribution rather than relying only on representative images.
2.3 Main Limitations of LC3 Detection
(1) Not flux-specific
Increased LC3-II and LC3 puncta cannot independently distinguish enhanced autophagy induction from degradation blockade.
(2) Interference from noncanonical LC3-related processes
LC3 may participate in LC3-associated phagocytosis, endosomal membrane modification, and certain noncanonical membrane processes. In immune cells, phagocytes, infection models, and membrane-trafficking abnormality models, LC3-positive structures do not necessarily represent classical autophagosomes.
(3) Strong time dependence
Autophagy is a dynamic process. At different time points, LC3-II may first increase and then decrease, while p62 may first accumulate and then degrade. A time-course design is therefore preferable to testing a single endpoint.
Table 2 Comparison of LC3-Related Detection Methods
Method | Detection object | Main advantage | Main limitation | Recommended use |
LC3 Western blot | LC3-I, LC3-II | Relatively clear quantification, suitable for flux experiments | Requires interpretation with lysosomal blockade | Autophagosome formation and flux analysis |
LC3 immunofluorescence | LC3 puncta | Allows observation of spatial distribution | Cannot independently determine flux | Autophagosome localization and intracellular distribution |
GFP-LC3 reporter system | LC3-positive membrane structures | Suitable for imaging and dynamic observation | Overexpression may cause aggregation | Observation of autophagosome formation |
LC3 immunohistochemistry | LC3 expression in tissue sections | Preserves tissue localization | Limited quantification and flux interpretation | Autophagy-related localization in tissue samples |
LC3 and LAMP1 colocalization | Relationship between autophagosomes and lysosomes | May indicate fusion-stage changes | Colocalization does not equal completed degradation | Autophagosome maturation analysis |
3、p62/SQSTM1 and Autophagic Substrate Detection
3.1 Detection of p62 Protein Level
(1) Detection principle
p62/SQSTM1 is a selective autophagy receptor that binds ubiquitinated substrates and interacts with LC3 through its LC3-interacting region. It is subsequently delivered to lysosomes for degradation during autophagy. Therefore, p62 protein level is often used to evaluate autophagic substrate clearance.
(2) Result interpretation
Increased LC3-II accompanied by decreased p62 usually supports enhanced autophagic flux. Increased LC3-II accompanied by increased p62 suggests autophagic substrate accumulation or impaired lysosomal degradation. If p62 decreases but LC3-II shows no obvious change, p62 transcriptional suppression, reduced protein synthesis, or other degradation pathways should be considered.
(3) Technical points
p62 is regulated by Nrf2, NF-κB, oxidative stress, inflammatory stimulation, and proteostasis stress. It is recommended to detect both p62 protein and SQSTM1 mRNA to distinguish transcriptional regulation from autophagy-mediated protein degradation.
3.2 Detection of Selective Autophagy Substrates
(1) NBR1
NBR1 is similar to p62 and can serve as an auxiliary indicator of selective autophagy substrates. NBR1 reduction may support enhanced substrate degradation, but it still requires interpretation together with LC3 and flux experiments.
(2) Ubiquitinated protein aggregates
When autophagy is blocked, ubiquitinated proteins and insoluble protein aggregates may accumulate. Protein quality control status can be evaluated by Western blot of ubiquitinated proteins, immunofluorescence, or insoluble protein fraction analysis.
(3) Specific organelle substrates
Selective autophagy should be evaluated around the target organelle. Mitophagy can be assessed using TOM20, COX IV, VDAC, PINK1, and Parkin. ER-phagy can be assessed using ER-phagy receptors and ER marker proteins. Lipophagy requires integration of lipid droplet staining, LC3 colocalization, and lipid metabolism indicators.
Table 3 Indicators for Autophagic Substrate Detection
Indicator | Common methods | Meaning of change | Interpretation notes |
p62/SQSTM1 | Western blot, immunofluorescence, immunohistochemistry | Decrease suggests enhanced substrate degradation; increase suggests substrate accumulation or blockade | Regulated by transcription and stress signaling |
NBR1 | Western blot, immunofluorescence | Assists evaluation of selective autophagy substrate degradation | Should not be used alone as a flux indicator |
Ubiquitinated proteins | Western blot, immunofluorescence | Accumulation suggests protein degradation stress or autophagy blockade | Proteasome activity also affects results |
TOM20/COX IV/VDAC | Western blot, immunofluorescence | Reduction may suggest mitochondrial clearance | Must be combined with mitochondrial mass and cell viability |
Insoluble protein aggregates | Fraction extraction, immunofluorescence | Aggregate accumulation suggests proteostasis abnormality | Need to distinguish autophagy from proteasome effects |
4、Autophagic Flux Detection Methods
4.1 Lysosomal Inhibitor Method
(1) Detection principle
The core of autophagic flux detection is comparing LC3-II or autophagic substrates before and after lysosomal inhibitor treatment. Common reagents include Bafilomycin A1, chloroquine, hydroxychloroquine, NH4Cl, and lysosomal protease inhibitors. If LC3-II further accumulates after lysosomal degradation is blocked, this indicates that autophagosomes continue to form and enter the degradation process.
(2) Result interpretation
If LC3-II increases in the treatment group and increases further after adding a lysosomal inhibitor, enhanced autophagic flux is supported. If LC3-II is already elevated but the inhibitor does not further increase it, blockade at the autophagic degradation stage should be considered. p62 usually accumulates in the presence of lysosomal inhibitors; if it does not accumulate, treatment time, protein synthesis, and detection sensitivity should be checked.
(3) Technical points
Inhibitor concentration and treatment time should be determined by pilot experiments. Bafilomycin A1 inhibits lysosomal acidification and may affect autophagosome-lysosome fusion-related processes. Chloroquine raises lysosomal pH but may also affect endocytosis, membrane trafficking, and cell toxicity. Flux experiments should avoid prolonged treatment that causes secondary cell injury.
4.2 mRFP-GFP-LC3 Dual-Fluorescence System
(1) Detection principle
mRFP-GFP-LC3 uses the fact that GFP is sensitive to acidic environments whereas RFP is relatively acid-resistant to distinguish autophagosomes from autolysosomes. In neutral autophagosomes, both GFP and RFP signals are present, appearing as yellow puncta. After entry into acidic autolysosomes, the GFP signal is quenched and mainly red puncta remain.
(2) Result interpretation
An increase in yellow puncta suggests increased autophagosomes. An increase in red puncta suggests autophagosomes have entered acidic lysosomes and formed autolysosomes. If yellow puncta increase markedly but red puncta do not, autophagosome-lysosome fusion impairment or abnormal lysosomal acidification should be considered.
(3) Technical points
Expression level of the reporter protein should be controlled to avoid nonspecific aggregation caused by overexpression. Imaging parameters should be kept consistent, and starvation induction, lysosomal blockade, and untreated controls should be included. Quantification should separately count yellow puncta, red puncta, and the red/yellow puncta ratio.
4.3 GFP-LC3-RFP-LC3ΔG System
(1) Detection principle
This system uses the feature that GFP-LC3 can be degraded by autophagy, whereas RFP-LC3ΔG does not participate in autophagic degradation. The GFP/RFP ratio is used to reflect autophagic flux. When autophagy is enhanced, GFP-LC3 degradation increases and the GFP/RFP ratio decreases.
(2) Application characteristics
This method is suitable for quantitative assessment of autophagic flux changes and can reduce the subjectivity of simple puncta counting. It is suitable for drug screening, genetic intervention, and dynamic flux analysis.
(3) Notes
Stable expression of the reporter system must be ensured, and the effects of treatment on GFP/RFP protein expression, translation efficiency, fluorescence stability, and cell viability must be excluded.
Table 4 Comparison of Autophagic Flux Detection Methods
Method | Detection logic | Main advantage | Main limitation | Application scenario |
LC3-II plus lysosomal inhibitor | Compare LC3-II accumulation before and after blockade | Direct flux interpretation, suitable for Western blot | Inhibitors may cause cytotoxicity and nonspecific effects | Routine autophagic flux detection |
p62 plus lysosomal inhibitor | Compare whether substrate degradation is blocked | Observes substrate clearance status | p62 is affected by transcriptional regulation | Auxiliary judgment of substrate degradation |
mRFP-GFP-LC3 | Distinguishes autophagosomes from autolysosomes | Visualizes flux process | Depends on transfection and imaging quality | Live-cell or fixed-cell imaging |
GFP-LC3-RFP-LC3ΔG | Uses fluorescence ratio to reflect flux | Suitable for quantification and screening | Requires stable reporter system | Drug screening, mechanism studies |
LC3 and LAMP1 colocalization | Assesses relationship between autophagosomes and lysosomes | Provides relatively clear spatial information | Colocalization does not equal completed degradation | Fusion-stage analysis |
5、Lysosomal Function and Fluorescent Dye Detection
5.1 LysoTracker and LysoSensor
(1) Detection principle
LysoTracker and LysoSensor label acidic organelles and are used to observe lysosomal acidification and acidic compartment changes. Autophagy ultimately depends on lysosomal degradation, so abnormal lysosomal acidification directly affects autophagic flux.
(2) Result interpretation
Enhanced acidic lysosomal signal may indicate increased lysosome number or acidification, but may also result from lysosomal accumulation, damage, or autophagy blockade. If LC3-II elevation is accompanied by abnormally enhanced LysoTracker signal and p62 accumulation, blockade at the autophagic degradation stage should be considered.
(3) Notes
LysoTracker is not an autophagy-specific dye and can only serve as a lysosomal status indicator. Dye concentration, incubation time, cell density, and imaging parameters all affect signal intensity.
5.2 MDC and Cyto-ID
(1) MDC staining
MDC can label autophagic vacuole-like structures, but its specificity is limited and it is easily affected by other membranous structures. MDC alone cannot provide sufficient evidence for autophagy occurrence or enhanced flux.
(2) Cyto-ID staining
Cyto-ID can be used to detect autophagy-related vesicles and is commonly used for flow cytometry or fluorescence microscopy. Its advantage is operational simplicity and suitability for screening, but verification with LC3, p62, or flux experiments is still required.
(3) Interpretation principle
Fluorescent dye-based methods are suitable for rapid screening and auxiliary observation. They should not replace LC3-II, p62, and autophagic flux detection. If dye signal increases but classical autophagy indicators do not support the conclusion, interpretation should be cautious.
5.3 Lysosomal Proteins and Enzyme Activity Detection
(1) Cathepsin activity
Activities of lysosomal proteases such as Cathepsin B, Cathepsin D, and Cathepsin L reflect degradation capacity. If autophagosome formation is normal but cathepsin activity decreases, autophagic substrates may still fail to degrade efficiently.
(2) LAMP1/LAMP2
LAMP1 and LAMP2 are lysosome-associated membrane proteins and can be used to observe lysosome number, distribution, and colocalization with LC3-positive structures. LAMP2 abnormalities may affect autophagosome-lysosome fusion and substrate degradation.
(3) Lysosomal pH
Lysosomal acidification is essential for autophagic degradation. Drug treatment, genetic intervention, or cell damage that raises lysosomal pH may cause p62 accumulation, LC3-II elevation, and impaired substrate clearance.
Table 5 Lysosome- and Autophagy-Related Fluorescent Detection Methods
Method | Detection object | Relationship with autophagy | Limitation |
LysoTracker | Acidic lysosomal compartments | Reflects lysosome number and acidification status | Not autophagy-specific |
LysoSensor | Changes in lysosomal pH | Determines whether lysosomal acidification is abnormal | Affected by dye conditions and imaging parameters |
MDC | Autophagic vacuole-like structures | Can assist observation of autophagy-related vesicles | Low specificity |
Cyto-ID | Autophagy-related vesicles | Suitable for screening and flow cytometry | Requires validation with classical indicators |
Cathepsin activity assay | Lysosomal protease function | Assesses substrate degradation capacity | Does not reflect autophagy initiation |
LAMP1/LAMP2 immunofluorescence | Lysosomal membrane structures | Can analyze autophagosome-lysosome relationship | Colocalization does not equal completed degradation |
6、Electron Microscopy Detection
6.1 Detection Value
(1) Ultrastructural observation
Transmission electron microscopy can directly observe double-membrane autophagosomes, single-membrane autolysosomes, membranous structures engulfing cytoplasmic contents, and vesicle morphology at different degradation stages. It is an important method for confirming autophagy-related structures.
(2) Structural resolution advantage
Electron microscopy can observe organelle damage, mitochondrial engulfment, membranous structure formation, and degradation contents inside lysosomes. It has high value for mitophagy, organelle-selective autophagy, and ultrastructural analysis of tissue samples.
6.2 Interpretation Points
(1) Autophagosomes
Typical autophagosomes are double-membrane structures containing undegraded cytoplasmic components or organelles. Single-membrane vacuoles or ordinary lysosomes alone should not be directly defined as autophagosomes.
(2) Autolysosomes
Autolysosomes are mostly single-membrane structures containing degrading cytoplasmic components with heterogeneous electron density. Their presence suggests that autophagosomes have entered the degradation stage, but still does not provide quantitative flux information alone.
(3) Quantification methods
The number of autophagosomes/autolysosomes per cell, number of autophagic structures per unit area, or proportion of autophagic vesicles containing mitochondria can be counted. Sample fixation, sampling region, section quality, and field selection significantly affect results.
6.3 Limitations
Electron microscopy requires demanding sample preparation, provides limited flux information, and only covers limited observation fields. It should be used as a structural validation method rather than the sole basis for autophagy detection. If autophagosome accumulation is observed by electron microscopy, LC3-II, p62, and lysosomal blockade experiments are still needed to evaluate autophagic flux.
Table 6 Interpretation of Autophagic Structures Under Electron Microscopy
Structure type | Morphological features | Biological meaning | Interpretation notes |
Autophagosome | Double membrane, engulfing cytoplasm or organelles | Autophagosome formation | Must be distinguished from ordinary vacuoles |
Autolysosome | Single membrane, contains degradation material | Autophagosome has entered degradation stage | Cannot independently quantify flux |
Mitochondria-containing structure | Mitochondrion surrounded by membranous structure | May suggest mitophagy | Should be combined with mitochondrial markers |
Vacuole-like structure | Irregular morphology, few contents | May represent damage or nonspecific vacuoles | Should not be directly defined as autophagy |
Increased lysosomes | High electron density or complex contents | Active or impaired degradation system | Requires lysosomal function testing |
7、Molecular-Level and Signaling Pathway Detection
7.1 Autophagy-Related Proteins
(1) ATG proteins
ATG5, ATG7, ATG12, ATG16L1, and other proteins participate in autophagosome formation. Their expression changes or gene knockdown can be used to verify autophagy dependence. If a treatment increases LC3-II and this change disappears after ATG5 or ATG7 knockdown, the process is more likely to depend on the classical autophagy pathway.
(2) Beclin 1
Beclin 1 participates in autophagy initiation and membrane nucleation. Changes in Beclin 1 may suggest the regulatory status of autophagy initiation, but cannot independently represent changes in autophagic flux.
(3) ULK1 and mTOR/AMPK signaling
mTOR inhibition, AMPK activation, and changes in ULK1 phosphorylation may indicate regulation of autophagy by nutrient and energy-sensing pathways. Starvation, rapamycin, Torin1, and energy stress often affect autophagy through these pathways. Signaling pathway indicators should be interpreted together with LC3, p62, and flux experiments.
7.2 mRNA Detection
(1) Applicable scope
qPCR can detect changes in MAP1LC3, BECN1, ATG5, ATG7, SQSTM1, and other gene expression levels, and is used to analyze the transcriptional regulatory background of autophagy.
(2) Limitations
Autophagy is primarily a dynamic degradation process, and mRNA expression cannot directly reflect autophagic flux. Especially when SQSTM1 mRNA is upregulated, p62 protein may not decrease significantly even if autophagic degradation is enhanced.
7.3 Genetic Validation
(1) Gene knockdown or knockout
siRNA, shRNA, CRISPR, and other approaches can be used to knock down ATG5, ATG7, BECN1, and ULK1 to verify whether a phenotype depends on autophagy.
(2) Functional rescue
If autophagy phenotypes and cellular functional changes are restored by re-expressing the relevant gene in a knockdown background, the credibility of the mechanistic conclusion is strengthened.
(3) Selective autophagy validation
For mitophagy, ER-phagy, lipophagy, and other forms of selective autophagy, specific receptors, organelle markers, and colocalization analysis must be combined. Total LC3 changes alone are insufficient.
Table 7 Molecular-Level Detection Indicators
Detection category | Common indicators | What it can indicate | Main limitation |
Autophagy initiation | ULK1, Beclin 1, VPS34 | Whether initiation signals are regulated | Cannot directly indicate flux |
Autophagosome formation | ATG5, ATG7, ATG12, ATG16L1 | Whether autophagy machinery participates | Expression changes do not equal functional changes |
mTOR/AMPK signaling | p-mTOR, p-AMPK, p-ULK1 | Nutrient and energy signaling regulation | Pathways are complex and require functional experiments |
Transcriptional detection | MAP1LC3, SQSTM1, BECN1 mRNA | Transcriptional regulatory background | Cannot replace protein-level flux detection |
Genetic validation | ATG5/ATG7 knockdown or knockout | Autophagy dependence | May cause long-term adaptive changes |
8、Product Selection for Cell Autophagy Detection
Table 8 Autophagy Induction and Inhibition Reagents
Cat. No. | Product Name | Grade/Specification | Applicable detection stage | Application positioning |
Earle's Balanced Salt Solution (with Ca2+xa0& Mg2+) |
| Starvation/nutrient deprivation induction | Used to establish nutrient stress or autophagy induction conditions; can serve as a basic treatment system for autophagy induction experiments | |
STF-62247 | ≥98% | Autophagy induction | Used for pharmacological autophagy induction, suitable for combination with LC3-II, p62, and flux assays | |
Autophagy Compound Library |
| Autophagy regulation screening | Used for screening autophagy inducers, inhibitors, or regulatory compounds | |
Rapamycin (AY-22989) | Moligand™, 10mM in DMSO | Autophagy induction control | Used for mTOR-dependent autophagy induction; commonly used as a positive control | |
Rapamycin | Moligand™, ≥98%(HPLC) | Autophagy induction control | Used as a positive inducer in Western blot, fluorescence imaging, and flux assays | |
Rapamycin | Moligand™, ≥95%(HPLC) | Autophagy induction | Used in mTOR inhibition-related autophagy studies | |
Torin 1 | Moligand™, 2mM in DMSO | Autophagy induction | Used for studies of autophagy activation related to mTORC1/2 inhibition | |
D-(+)-Trehalose Anhydrous | ≥99% | mTOR-independent autophagy induction | Used for mTOR-independent autophagy induction studies | |
D-(+)-Trehalose Anhydrous | 10mM in DMSO | Autophagy induction | Used for comparison of autophagy induction conditions | |
3-Methyladenine | autophagy inhibitor | Autophagy initiation/nucleation blockade | Used for PI3K-related autophagy initiation inhibition and autophagy-dependence validation | |
3-Methyladenine | 10mM in DMSO | Autophagy initiation/nucleation blockade | Used for pharmacological blockade of autophagosome formation | |
3-Methyladenine | ≥98% | Autophagy initiation/nucleation blockade | Used as an early autophagy inhibition control | |
Wortmannin (KY 12420) | Moligand™, 10mM in DMSO | Autophagy initiation inhibition | Used for intervention in VPS34/PI3K-related autophagy initiation stages | |
Wortmannin | Moligand™, ≥98% | Autophagy initiation inhibition | Used to validate blockade of the autophagosome formation stage | |
ATG7-IN-1 | ≥99% | Autophagosome formation intervention | Used for inhibition of ATG7-dependent autophagy processes | |
ATG7-IN-2 | Moligand™, 10 mM in DMSO | Autophagosome formation intervention | Used for pharmacological inhibition experiments involving ATG7 | |
ATG7-IN-2 | ≥99% | Autophagosome formation intervention | Used for ATG7-dependent mechanism validation | |
ATG7-IN-3 | ≥99% | Autophagosome formation intervention | Used for ATG7-related autophagy inhibition studies | |
Beclin1-ATG14L interaction inhibitor 1 | ≥99% | Autophagy initiation/membrane nucleation intervention | Used for studies of autophagy mechanisms related to Beclin1-ATG14L interaction | |
Beclin1-Bcl-2 interaction inhibitor 1 |
| Autophagy initiation regulation | Used for studies of Beclin1-Bcl-2 axis-related autophagy regulation | |
Tat-beclin 1 | ≥99% | Autophagy induction | Used for Beclin 1-related autophagy induction studies | |
Tat-beclin 1 acetate(Tat-BECN1 acetate) | ≥98% | Autophagy induction | Used to induce autophagy and validate Beclin 1-related pathways | |
Tat-beclin 1 scrambled | ≥99% | Autophagy induction control | Used as a sequence control in Tat-beclin 1-related experiments | |
Tat-beclin 1 scrambled TFA | ≥98% | Autophagy induction control | Used to exclude nonspecific effects of Tat-beclin 1 |
Table 9 Autophagy Staining, Lysosomal Function, and Fluorescence Imaging Reagents
Cat. No. | Product Name | Grade/Specification | Applicable detection stage | Application positioning |
Autophagy/Cytotoxicity Dual-Color Detection Kit (MDC/PI Method) | BioReagent,Biological Stain,for microscopy,sterile,for fluorescence analysis | Autophagic vacuole-like structures/cytotoxicity | Used to label autophagy-related vesicles with MDC and evaluate cytotoxicity with PI | |
Autophagy Staining and Detection Kit (MDC Method) | BioReagent,Biological Stain,for microscopy | Autophagic vacuole-like structures | Used for rapid fluorescence observation of autophagy-related vesicles; requires LC3/p62 validation | |
Autophagy Green Detection Kit (MDC Method) | BioReagent,Biological Stain,for microscopy,sterile,for fluorescence analysis | Autophagic vacuole-like structures | Used for green fluorescence detection of autophagy-related vesicles; suitable for microscopy and screening assays | |
LysoTracker Blue DND-22 |
| Lysosomal acidification/localization | Used for acidic lysosomal compartment labeling and auxiliary assessment of the autophagic degradation stage | |
LysoTracker Red | ≥97% | Lysosomal acidification/localization | Used for lysosome localization and colocalization analysis with LC3 and p62 | |
LysoTracker Yellow HCK 123 | ≥98% | Lysosomal acidification/localization | Used to observe acidic lysosomal compartments | |
LysoSensor PDMPO | ≥98% | Lysosomal acidification function | Used to evaluate lysosomal pH changes and autophagic degradation conditions | |
Hoechst 33342 Staining Solution | Suitable for Immunofluorescence(IF), BioReagent, ready-to-use, Biological Stain, for fluorescence analysis, Biological dye grade, for microscopy, for cell culture, 1.0 mg/ml in H₂O | Fluorescence imaging auxiliary localization | Used for nuclear localization and cell counting in LC3, p62, LAMP1, and other immunofluorescence assays | |
bisBenzimide H 33342 trihydrochloride | 10mM in DMSO | Fluorescence imaging auxiliary localization | Used for nuclear staining of live or fixed cells | |
bisBenzimide H 33342 trihydrochloride | ≥98% | Fluorescence imaging auxiliary localization | Used for cell nuclear localization in autophagy fluorescence detection | |
Bisbenzimide H 33342 Fluorochrome, Trihydrochloride | Cell-permeable, adenine-thymine-specific fluorescent stain. | Fluorescence imaging auxiliary localization | Used for nuclear staining and image normalization | |
4',6-Diamidino-2-phenylindole Dihydrochloride | ≥97% | Fluorescence imaging auxiliary localization | Used for nuclear localization in immunofluorescence | |
4',6-Diamidino-2-phenylindole Dihydrochloride | ≥98% | Fluorescence imaging auxiliary localization | Used for nuclear counterstaining in LC3/p62/LAMP1 colocalization imaging | |
4',6-Diamidino-2-phenylindole Dihydrochloride | 10mM in DMSO | Fluorescence imaging auxiliary localization | Used for nuclear staining in autophagy-related immunofluorescence experiments | |
DAPI staining solution (ready to use) |
| Fluorescence imaging auxiliary localization | Used for nuclear localization and cell counting in autophagy fluorescence imaging |
Table 10 LC3- and p62-Related Detection Tools
Cat. No. | Product Name | Grade/Specification | Applicable detection stage | Application positioning |
AAV-mCherry-GFP-LC3B (AAV9) | 10^13vp/ml | Autophagic flux | Used to distinguish autophagosomes from autolysosomes; suitable for flux observation in cells or animal models | |
Ad-GFP-LC3B |
| Autophagosome formation | Used to observe GFP-LC3B puncta and autophagosome formation | |
Ad-mCherry-GFP-LC3B |
| Autophagic flux | Used to distinguish autophagosomes and autolysosomes by yellow/red puncta | |
AdPlus-mCherry-GFP-LC3B |
| Autophagic flux | Used for imaging autophagosome maturation and lysosomal fusion | |
Lenti-EGFP-LC3B | 10^9TU/ml | Autophagosome formation | Used to establish stable LC3B reporter cell lines | |
Lenti-mCherry-EGFP-LC3B | 10^9TU/ml | Autophagic flux | Used for autophagic flux observation in stable expression systems | |
pCMV-GFP-LC3B |
| Autophagosome formation | Used for transient expression of GFP-LC3B and observation of LC3 puncta | |
pCMV-mCherry-GFP-LC3B |
| Autophagic flux | Used to distinguish autophagosomes from autolysosomes | |
LC3B Mouse mAb | Carrier Free,ExactAb™,Azide Free,Validated,High Performance,PBS Only,≥95%(SDS-PAGE),1.0 mg/mL | LC3 Western blot/immunofluorescence/immunohistochemistry | Used to detect LC3-II changes or LC3 puncta; a core antibody for autophagy detection | |
Recombinant LC3B Antibody | Recombinant, ExactAb™, Validated, See COA | LC3 detection | Used for LC3B protein expression, localization, and autophagosome formation analysis | |
Recombinant MAP1LC3B Antibody | KD Validation | LC3 detection | Suitable for validating antibody specificity in MAP1LC3B knockdown systems | |
MAP1LC3B Human Pre-designed siRNA Set A |
| Autophagy-dependence validation | Used to knock down LC3B and validate LC3-related phenotypes | |
MAP1LC3B2 Human Pre-designed siRNA Set A |
| Autophagy-dependence validation | Used for LC3B2-related autophagy mechanism studies | |
Human Microtubule-associated Protein Light Chain 3B(LC3B) ELISA Kit | BioReagent | LC3B quantification | Used to detect LC3B levels in human-derived samples | |
Rat Microtubule-Associated Proteins 1A/1B Light Chain 3B (MAP1LC3b) ELISA Kit | BioReagent | LC3B quantification | Used to detect LC3B levels in rat samples | |
Ad-GFP-p62 |
| Autophagic substrate localization | Used to observe p62 aggregation, substrate recognition, and selective autophagy-related localization | |
Ad-mCherry-p62 |
| Autophagic substrate localization | Used to observe p62-positive aggregates and autophagic substrate localization | |
pCMV-GFP-p62 |
| Autophagic substrate localization | Used for GFP-p62 expression and p62 aggregate imaging | |
pCMV-mCherry-p62 |
| Autophagic substrate localization | Used to observe p62 selective autophagy substrate localization | |
SQSTM1 Human Pre-designed siRNA Set A |
| p62-dependence validation | Used to knock down p62 and validate selective autophagy-related mechanisms | |
SQSTM1 Mouse mAb | Carrier Free, ExactAb™, Validated, High Performance, See COA | Autophagic substrate degradation detection | Used to detect p62 levels by Western blot, immunofluorescence, or immunohistochemistry | |
Human Sequestosome 1 (SQSTM1) ELISA Kit | BioReagent | p62 quantification | Used to detect p62/SQSTM1 levels in human-derived samples | |
Rat Sequestosome 1 (SQSTM1) ELISA Kit | BioReagent | p62 quantification | Used to detect p62/SQSTM1 levels in rat samples |
Table 11 Beclin 1-, ATG-, and ULK1-Related Detection Tools
Cat. No. | Product Name | Grade/Specification | Applicable detection stage | Application positioning |
Beclin 1 Mouse mAb | Carrier Free,ExactAb™,Azide Free,Validated,High Performance,PBS Only,≥95%(SDS-PAGE),1.0 mg/mL | Autophagy initiation detection | Used to detect Beclin 1, a protein related to autophagy initiation and membrane nucleation | |
Recombinant Beclin 1 Antibody | KD Validation | Autophagy initiation detection | Suitable for detecting Beclin 1 signals in knockdown validation systems | |
Recombinant Beclin 1 Antibody | KD Validation | Autophagy initiation detection | Used for Beclin 1 expression and autophagy initiation analysis | |
Recombinant Beclin 1 Antibody | Recombinant, ExactAb™, Validated, See COA | Autophagy initiation detection | Used to detect Beclin 1 by Western blot or immunostaining | |
Human Phosphorylated Serine/threonine-Protein kinase ULK1 (P-ULK1) ELISA Kit | BioReagent | Autophagy initiation signal detection | Used to quantify ULK1 phosphorylation and reflect autophagy initiation regulation | |
Human Autophagy-related Protein 3 (ATG3) ELISA Kit | BioReagent | Autophagosome formation-related detection | Used to detect ATG3 levels and assist evaluation of LC3 lipidation-related processes | |
ATG5 Antibody | KD Validation | Autophagosome formation detection | Used to detect ATG5 and classical autophagosome formation mechanisms | |
Recombinant APG5L/ATG5 Antibody | ExactAb™, Validated, Recombinant, 0.3 mg/mL | Autophagosome formation detection | Used for ATG5 expression detection and autophagy-dependence validation | |
Recombinant ATG5 Antibody | KD Validation | Autophagosome formation detection | Suitable for ATG5 detection in knockdown validation contexts | |
ATG5 Human Pre-designed siRNA Set A |
| Autophagy-dependence validation | Used to knock down ATG5 and validate dependence on the classical autophagy pathway | |
pLenti-ATG5-sgRNA |
| Antibody validation/mechanism control | Used for ATG5 antibody validation and negative controls | |
pLenti-ATG5-sgRNA |
| RNA detection control | Used as a transcriptional detection control in an ATG5 knockout background | |
Human Autophagy Related Protein 5 (ATG5) ELISA Kit | BioReagent | Autophagosome formation-related detection | Used to detect ATG5 levels in human-derived samples | |
ATG7 Antibody | ExactAb™, Validated, 0.6 mg/mL | Autophagosome formation detection | Used to detect ATG7 expression and analyze LC3 lipidation-related mechanisms | |
Recombinant ATG7 Antibody | KD Validation | Autophagosome formation detection | Suitable for antibody validation in ATG7 knockdown systems | |
Recombinant ATG7 Antibody | KD Validation | Autophagosome formation detection | Used for ATG7-related autophagy mechanism studies | |
ATG7 Human Pre-designed siRNA Set A |
| Autophagy-dependence validation | Used to knock down ATG7 and validate classical autophagy dependence |
Table 12 Lysosomal Markers, Proteases, and Mitophagy-Related Tools
Cat. No. | Product Name | Grade/Specification | Applicable detection stage | Application positioning |
LAMP1 /CD107a Antibody | KD Validation | Lysosomal localization/autophagy fusion | Used to detect the lysosomal membrane marker LAMP1 | |
LAMP1 Mouse mAb | Carrier Free,ExactAb™,Azide Free,Validated,≥95%(SDS-PAGE),1.0 mg/mL | Lysosomal localization | Used for LC3-LAMP1 colocalization and lysosome number analysis | |
LAMP1/CD107a Mouse mAb | See COA | Lysosomal localization | Used for analysis of autophagosome-lysosome fusion | |
LAMP1 Human Pre-designed siRNA Set A |
| Lysosomal function validation | Used to knock down LAMP1 and analyze lysosomal/autophagic fusion stages | |
pLenti-LAMP1-sgRNA |
| Antibody validation/mechanism control | Used for LAMP1 antibody validation and negative controls | |
pLenti-LAMP1-sgRNA |
| RNA detection control | Used for transcriptional detection in a LAMP1 knockout background | |
Recombinant LAMP2 Antibody | ExactAb™, Validated, Recombinant, 0.8 mg/mL | Lysosomal function detection | Used for LAMP2 expression, localization, and lysosome-related autophagic degradation analysis | |
Recombinant LAMP2 Antibody | KD Validation | Lysosomal function detection | Suitable for detection in LAMP2 knockdown validation contexts | |
LAMP2 Human Pre-designed siRNA Set A |
| Lysosomal function validation | Used to validate LAMP2-dependent autophagosome-lysosome function | |
Human Lysosomal Associated Membrane Protein 2 (LAMP2) ELISA Kit | BioReagent | Lysosomal marker quantification | Used to detect LAMP2 levels in human-derived samples | |
Cathepsin D LC Antibody | KD Validation | Lysosomal degradation function | Used to detect lysosomal protease-related degradation capacity | |
Cathepsin D Mouse mAb | Carrier Free,ExactAb™,Azide Free,Validated,High Performance,PBS Only,≥95%(SDS-PAGE),1.0 mg/mL | Lysosomal protease detection | Used for Cathepsin D expression and maturation analysis | |
Cathepsin D and E FRET Substrate acetate | ≥98% | Lysosomal protease activity | Used for Cathepsin D/E enzyme activity detection and auxiliary evaluation of lysosomal degradation function | |
Cathepsin D/E Substrate, Fluorogenic |
| Lysosomal protease activity | Used for fluorescence-based detection of Cathepsin D/E activity | |
PINK1 Human Pre-designed siRNA Set A |
| Mitophagy validation | Used to knock down PINK1 and validate PINK1-dependent mitophagy | |
Human PTEN Induced Putative Kinase 1 (PINK1) ELISA Kit | BioReagent | Mitophagy marker quantification | Used to detect PINK1 levels in human-derived samples | |
Rat PTEN Induced Putative Kinase 1 (PINK1) ELISA Kit | BioReagent | Mitophagy marker quantification | Used to detect PINK1 levels in rat samples | |
Mouse PTEN-induced Putative Kinase 1(PINK1) ELISA Kit | BioReagent | Mitophagy marker quantification | Used to detect PINK1 levels in mouse samples | |
Recombinant Parkin Antibody | Recombinant, ExactAb™, Validated, See COA | Mitophagy detection | Used for PINK1/Parkin pathway-related mitophagy studies | |
Human Parkin Protein(PP) ELISA Kit | BioReagent | Mitophagy marker quantification | Used to detect Parkin protein levels in human-derived samples | |
CCCP solution (10mmol/L) | BioReagent,10 mmol/L | Mitophagy induction | Used to induce decreased mitochondrial membrane potential and establish PINK1/Parkin-dependent mitophagy models | |
Carbonyl cyanide 3-chlorophenylhydrazone | 10mM in DMSO | Mitophagy induction | Used for mitochondrial depolarization and mitophagy induction | |
Carbonyl cyanide 3-chlorophenylhydrazone (CCCP) | Moligand™, ≥98% | Mitophagy induction | Used for PINK1/Parkin pathway and mitochondrial clearance experiments | |
MitoTracker Deep Red FM | ≥99% | Mitochondrial localization/mitophagy | Used for mitochondrial mass, distribution, and colocalization analysis with LC3/LAMP1 | |
MitoTracker Orange CMTMRos |
| Mitochondrial localization/membrane potential-related observation | Used for mitochondrial structure and mitophagy-related colocalization analysis | |
Nile Red | BioReagent, for fluorescence analysis, ≥95%(HPLC) | Auxiliary lipophagy detection | Used for lipid droplet staining and can be combined with LC3/LAMP1 colocalization to analyze lipophagy | |
Oil red O | 10mM in DMSO | Auxiliary lipophagy detection | Used for lipid accumulation observation; lipophagy interpretation requires autophagic flux indicators | |
Oil red O(C.1.26125) | Biological Stain | Auxiliary lipophagy detection | Used for lipid droplet and neutral lipid staining; suitable for lipophagy background observation |
Cell autophagy detection should be designed around autophagic flux. LC3-II, p62, autophagy reporter systems, lysosomal function assays, and electron microscopy each reflect different stages. Only combined application can distinguish enhanced autophagy induction, autophagosome accumulation, and impaired lysosomal degradation.
For more related articles, please see below:
[1] Methods of observation and detection of cellular autophagy processes
