At1g47390 Antibody

What is the At1g47390 gene and why is studying its protein product important?

At1g47390 encodes an F-box and associated interaction domains-containing protein in Arabidopsis thaliana (Mouse-ear cress) . F-box proteins typically function as substrate-recognition components within SCF (Skp, Cullin, F-box) ubiquitin ligase complexes, regulating protein degradation through the ubiquitin-proteasome pathway. These proteins play essential roles in diverse cellular processes including hormone signaling, development, and stress responses in plants. Understanding the precise function of the At1g47390 gene product requires specific antibodies to track its expression, localization, interactions, and post-translational modifications in various experimental contexts. Studying At1g47390 contributes to our broader understanding of protein-mediated signaling networks in plant development and environmental responses .

What are the key considerations when selecting an appropriate At1g47390 antibody for my research?

When selecting an At1g47390 antibody, researchers should consider multiple factors to ensure experimental success. First, verify the antibody's specificity through documentation of validation techniques such as Western blotting against wild-type and knockout mutants, immunoprecipitation followed by mass spectrometry, or ELISA testing against recombinant protein. Second, determine the appropriate antibody format (polyclonal vs. monoclonal) based on your experimental needs—polyclonals often provide higher sensitivity by recognizing multiple epitopes but with potential cross-reactivity, while monoclonals offer greater specificity but potentially lower sensitivity . Third, confirm the antibody's validated applications (Western blot, immunoprecipitation, immunohistochemistry, etc.) match your experimental requirements. Fourth, check the antibody's reactivity with specific Arabidopsis ecotypes, as protein sequence variations may affect epitope recognition. Finally, review literature citing the antibody to assess its performance in contexts similar to your experimental design .

How does the structure of an At1g47390 antibody influence its experimental applications?

The structure of an At1g47390 antibody fundamentally determines its experimental utility through its domain organization. Like all antibodies, it contains variable regions in the Fab portion that recognize specific epitopes on the At1g47390 protein, determining specificity and affinity. The heavy chain constant regions in the Fc portion influence experimental applications through interactions with secondary reagents, protein A/G, and complement proteins . Specifically, the paratope at each tip of the "Y" structure precisely binds to epitopes on the At1g47390 protein, enabling detection, quantification, and functional analysis . Additionally, glycosylation patterns in the Fc region can affect antibody stability and function in different experimental conditions. For instance, alterations in galactosylation levels can influence interactions with Fc receptors, potentially affecting immunoprecipitation efficiency . Understanding these structural features helps researchers optimize experimental conditions and interpret results when using At1g47390 antibodies in applications such as Western blotting, co-immunoprecipitation studies, or immunolocalization in plant tissues.

How should I design positive and negative controls when using At1g47390 antibody in Western blot experiments?

Rigorous control design is essential for reliable Western blot experiments with At1g47390 antibody. For positive controls, consider using protein extracts from Arabidopsis tissues with known high expression of At1g47390, recombinant At1g47390 protein with appropriate tags, or overexpression lines of At1g47390 generated through Agrobacterium-mediated transformation. These controls confirm antibody functionality and establish expected band size patterns . For negative controls, implement multiple approaches: include At1g47390 knockout or knockdown lines (T-DNA insertion mutants or CRISPR-edited lines) to demonstrate specificity; pre-absorb the antibody with purified recombinant At1g47390 protein to block specific binding; use secondary antibody-only controls to detect non-specific binding; and include protein extracts from tissues with minimal At1g47390 expression based on transcriptomic data . Additionally, incorporate loading controls targeting constitutively expressed proteins (e.g., actin, tubulin) to normalize expression data. When presenting Western blot data, include molecular weight markers and document all experiment parameters (protein amounts loaded, exposure times, antibody dilutions) to enhance reproducibility. This comprehensive control strategy enables confident interpretation of specific At1g47390 protein detection versus potential artifacts .

What are the optimal tissue preparation and protein extraction methods for detecting At1g47390 protein in different plant organs?

Optimizing tissue preparation and protein extraction for At1g47390 detection requires tissue-specific approaches due to varying protein expression levels, interfering compounds, and matrix effects across plant organs. For leaf tissue, rapid freezing in liquid nitrogen followed by grinding to fine powder is essential to prevent proteolytic degradation. Extract proteins using a buffer containing 50 mM Tris-HCl (pH 7.5), 150 mM NaCl, 1% Triton X-100, 0.5% sodium deoxycholate, and protease inhibitor cocktail . For root tissue, which contains higher levels of interfering phenolic compounds, incorporate polyvinylpolypyrrolidone (PVPP, 2% w/v) and β-mercaptoethanol (5 mM) in your extraction buffer to neutralize phenolics and prevent oxidation. When extracting from seeds or siliques, modify your approach by using a stronger buffer containing 7M urea, 2M thiourea, 4% CHAPS, and 1% DTT to solubilize more hydrophobic proteins . Subcellular fractionation may be necessary since F-box proteins like At1g47390 can shuttle between cytoplasm and nucleus; implement differential centrifugation protocols to isolate specific cellular compartments. To enhance detection sensitivity, consider concentrating low-abundance proteins through immunoprecipitation before Western blotting. Finally, validate your extraction protocol by quantifying total protein yield using Bradford or BCA assays and assessing extract quality by SDS-PAGE with Coomassie staining prior to immunoblotting with At1g47390 antibody .

How can I optimize immunoprecipitation protocols to study protein interactions with At1g47390?

Optimizing immunoprecipitation (IP) protocols for studying At1g47390 protein interactions requires careful consideration of multiple parameters. Begin by testing different lysis conditions to preserve protein-protein interactions; a standard starting buffer might contain 50 mM Tris-HCl (pH 7.5), 150 mM NaCl, 0.5% NP-40, and protease inhibitors, but may require adjustment based on interaction stability . Pre-clear lysates with protein A/G beads for 1 hour at 4°C to reduce non-specific binding. When coupling At1g47390 antibody to beads, determine optimal antibody concentration through titration experiments (typically 2-5 μg per reaction) and test both direct antibody addition and pre-coupling to protein A/G beads or magnetic beads conjugated with anti-IgG . Critical parameters include incubation time (4-16 hours at 4°C with gentle rotation) and washing stringency (3-5 washes with decreasing salt concentrations) . To enhance specificity for transient interactions, consider implementing crosslinking with formaldehyde (0.3-1%) or DSP (dithiobis(succinimidyl propionate), 1-2 mM) prior to cell lysis. For detecting interactions with other SCF complex components, supplement lysis buffers with phosphatase inhibitors and MG132 proteasome inhibitor (10-25 μM) to prevent degradation of ubiquitinated substrates . Validate results using reciprocal IPs when possible, and implement appropriate controls: pre-immune serum or isotype control antibodies, lysates from At1g47390 knockout plants, and competitive elution with recombinant At1g47390 protein. Finally, analyze co-immunoprecipitated proteins by mass spectrometry to identify novel interaction partners beyond expected SCF complex components .

How can I quantitatively assess At1g47390 protein expression levels across different developmental stages?

Quantitative assessment of At1g47390 protein expression across developmental stages requires a multi-faceted approach combining Western blotting, quantitative image analysis, and validation with complementary techniques. First, establish a standardized protein extraction protocol that maintains consistent efficiency across diverse tissue types and developmental stages, using phase-specific internal controls to normalize extraction yields . Develop a calibration curve using recombinant At1g47390 protein standards (5-100 ng) to establish linear detection ranges for your antibody. When performing quantitative Western blots, load equal total protein amounts (validated by BCA or Bradford assays) and include housekeeping protein controls appropriate for each developmental stage (note that traditional housekeeping proteins like actin may vary across development) . Implement technical replicates (minimum n=3) and biological replicates from independent plant populations. For image analysis, use software packages like ImageJ with background subtraction and normalization to housekeeping proteins to generate relative expression values . To validate Western blot results, correlate protein levels with transcript abundance using RT-qPCR, but recognize that post-transcriptional regulation may cause discrepancies. For absolute quantification, consider ELISA methods using the At1g47390 antibody or targeted proteomics approaches like selected reaction monitoring (SRM) or parallel reaction monitoring (PRM) mass spectrometry with isotope-labeled peptide standards derived from At1g47390. This multi-method approach enables robust quantitative tracking of At1g47390 protein dynamics throughout Arabidopsis development .

What approaches can detect post-translational modifications of the At1g47390 protein?

Detecting post-translational modifications (PTMs) of At1g47390 protein requires specialized methodologies that extend beyond conventional antibody applications. Begin with phosphorylation analysis by immunoprecipitating At1g47390 followed by Western blotting with phospho-specific antibodies (anti-phosphoserine, -threonine, or -tyrosine). Alternatively, treat samples with lambda phosphatase to confirm phosphorylation by observing mobility shifts in SDS-PAGE . For ubiquitination analysis, critical for F-box proteins which often undergo auto-ubiquitination, co-immunoprecipitate At1g47390 with anti-ubiquitin antibodies after treating plants with proteasome inhibitors (MG132, 50 μM, 4-6 hours) to prevent degradation of ubiquitinated forms . SUMOylation can be detected through similar co-IP approaches with anti-SUMO antibodies. For comprehensive PTM profiling, implement mass spectrometry-based approaches after enriching for modified peptides: titanium dioxide (TiO₂) enrichment for phosphopeptides, immunoaffinity enrichment for ubiquitinated or SUMOylated peptides, and lectin affinity chromatography for glycosylated forms . Site-specific PTM mapping can be achieved through targeted mass spectrometry methods like parallel reaction monitoring (PRM) focusing on predicted modification sites based on bioinformatic analysis of the At1g47390 sequence. Finally, investigate PTM dynamics in response to specific stimuli (hormones, stress conditions) by comparing modification patterns across treatment time courses, revealing regulatory mechanisms controlling At1g47390 function in plants .

How can I use At1g47390 antibody for chromatin immunoprecipitation (ChIP) to study protein-DNA interactions?

Implementing chromatin immunoprecipitation (ChIP) with At1g47390 antibody requires specific optimization for plant tissues and consideration of F-box protein biology. Begin with crosslinking optimization: test formaldehyde concentrations (1-3%) and fixation times (10-20 minutes) to balance efficient crosslinking with DNA recovery and epitope preservation . Tissue disruption requires careful optimization for Arabidopsis; use grinding in liquid nitrogen followed by nuclear isolation to reduce background from chloroplast and mitochondrial DNA. Sonication parameters (amplitude, cycle numbers, duration) must be calibrated to achieve chromatin fragments of 200-500 bp, verified by agarose gel electrophoresis . For immunoprecipitation, pre-clear chromatin with protein A/G beads and non-specific IgG to reduce background. As F-box proteins like At1g47390 typically function within SCF complexes rather than binding DNA directly, consider sequential ChIP (ChIP-reChIP) with antibodies against known transcription factors or chromatin modifiers that might mediate indirect DNA associations . Essential controls include: input DNA (non-immunoprecipitated chromatin), mock IP with non-specific IgG, positive control using antibodies against histone modifications (H3K4me3) or RNA polymerase II, and negative control regions in qPCR analysis . For data analysis, implement ChIP-qPCR targeting promoter regions of suspected target genes, calculating enrichment relative to input and IgG controls. For genome-wide profiling, perform ChIP-seq with appropriate sequencing depth (>20 million reads) and bioinformatic analysis to identify enriched regions. When interpreting results, remember that F-box proteins typically influence transcription indirectly through regulated degradation of transcription factors rather than through direct DNA binding .

What are the most common causes of non-specific binding when using At1g47390 antibody, and how can they be mitigated?

Non-specific binding when using At1g47390 antibody can arise from multiple sources requiring systematic troubleshooting. First, antibody quality issues may include heterogeneity in polyclonal preparations or degradation during storage; mitigate by using freshly aliquoted antibody, implementing more stringent affinity purification against the immunizing peptide, and validating with knockout controls . Second, blocking inefficiency can cause high background; optimize by testing different blocking agents (5% non-fat milk, 3-5% BSA, commercial blocking buffers) and extending blocking time (1-3 hours at room temperature) . Third, excessive antibody concentration increases non-specific interactions; perform titration experiments to determine minimal effective concentration (typically 0.5-2 μg/mL for Western blots) and extend incubation time at 4°C if needed . Fourth, cross-reactivity with related F-box proteins sharing sequence homology with At1g47390 may occur; implement more stringent washing conditions (higher salt concentration, 250-500 mM NaCl, or addition of 0.1% SDS to wash buffers) and pre-absorb antibody with recombinant proteins of closely related family members . Fifth, plant-specific interfering compounds like phenolics and polysaccharides can cause artifactual binding; modify extraction buffers with PVPP (2%) and increase concentration of non-ionic detergents like Triton X-100 (0.5-1%). Finally, secondary antibody cross-reactivity can create false positives; include secondary-only controls and consider using secondary antibodies pre-absorbed against plant proteins . Systematic evaluation of these parameters can substantially reduce non-specific binding and improve At1g47390 detection specificity.

How can I validate the specificity of At1g47390 antibody in my experimental system?

Validating At1g47390 antibody specificity requires implementing multiple complementary approaches. First, perform Western blot analysis comparing wild-type Arabidopsis extracts with genetic knockout lines (T-DNA insertion mutants or CRISPR-edited plants lacking At1g47390); the specific band should be absent or significantly reduced in knockout samples . Second, conduct peptide competition assays by pre-incubating the antibody with excess immunizing peptide or recombinant At1g47390 protein (10-100 fold molar excess); this should abolish specific signal while leaving non-specific binding unaffected . Third, verify antibody specificity across multiple experimental techniques (Western blot, immunoprecipitation, immunofluorescence) to ensure consistent recognition of the target protein. Fourth, implement molecular weight verification by comparing observed band size with theoretical molecular weight calculated from the At1g47390 sequence (accounting for potential post-translational modifications) . Fifth, perform heterologous expression validation by detecting At1g47390 protein in transfected/transformed systems (e.g., Arabidopsis protoplasts or Nicotiana benthamiana) expressing tagged versions of At1g47390, comparing antibody detection with anti-tag antibody detection. Sixth, conduct immunoprecipitation followed by mass spectrometry to confirm that the antibody enriches peptides derived from At1g47390. Finally, compare results with alternative antibodies raised against different epitopes of At1g47390 when available . This multi-faceted validation strategy provides robust confirmation of antibody specificity before proceeding with detailed experimental analyses.

What factors can lead to false negative results when using At1g47390 antibody, and how can detection sensitivity be improved?

False negative results with At1g47390 antibody can stem from multiple factors requiring systematic optimization. Epitope masking represents a primary concern; post-translational modifications, protein-protein interactions, or protein conformational changes may shield the epitope recognized by the antibody . To address this, test multiple protein denaturation conditions, including varying SDS concentrations (0.1-2%), reducing agent concentrations (5-100 mM DTT), and heat denaturation times (3-10 minutes at 95-100°C) . Protein degradation during extraction can eliminate detection; implement a comprehensive protease inhibitor cocktail, maintain samples at 4°C throughout processing, and consider adding deubiquitinase inhibitors (N-ethylmaleimide, 5 mM) to preserve ubiquitinated forms of F-box proteins . Low protein abundance often challenges detection; increase starting material (2-5 fold), implement protein concentration methods (TCA precipitation, methanol-chloroform precipitation), and consider using signal amplification systems like HRP-conjugated polymers or biotinylated secondary antibodies with streptavidin-HRP . Suboptimal transfer efficiency in Western blots can be addressed by optimizing transfer conditions (wet transfer for larger proteins, PVDF membranes for higher protein binding capacity, transfer time/voltage calibration) . To enhance sensitivity, implement extended antibody incubation (overnight at 4°C), optimize secondary antibody concentration, use high-sensitivity chemiluminescent substrates, increase exposure time incrementally, and consider alternative detection systems like infrared fluorescent secondary antibodies with scanning detection . Finally, consider enrichment before detection through immunoprecipitation or subcellular fractionation to concentrate At1g47390 from specific compartments where it may be more abundant. This comprehensive approach maximizes detection sensitivity while maintaining specificity .

How can I determine if changes in At1g47390 protein levels are due to transcriptional regulation or post-translational mechanisms?

Distinguishing between transcriptional and post-translational regulation of At1g47390 protein levels requires integrating multiple experimental approaches. Begin by performing parallel quantification of mRNA and protein levels across your experimental conditions using RT-qPCR and quantitative Western blotting with At1g47390 antibody, respectively . Concordant changes in mRNA and protein suggest transcriptional regulation, while discordant patterns indicate post-translational mechanisms. To specifically investigate protein stability, implement cycloheximide chase assays by treating plant tissues with cycloheximide (100-200 μg/mL) to inhibit new protein synthesis, then tracking At1g47390 protein degradation over a time course (0-24 hours) using Western blotting . Changes in degradation rate between experimental conditions would indicate altered post-translational regulation. To assess ubiquitin-mediated degradation, common for F-box proteins which often undergo autoubiquitination, treat plants with proteasome inhibitors (MG132, 50 μM, 4-12 hours) and compare At1g47390 accumulation patterns across conditions . For transcriptional analysis, examine At1g47390 promoter activity using promoter-reporter constructs (e.g., pAt1g47390:GUS or pAt1g47390:LUC) and complement with chromatin immunoprecipitation (ChIP) studies targeting transcription factors potentially regulating the At1g47390 promoter. Additionally, analyze At1g47390 mRNA stability through actinomycin D chase experiments, where transcription is blocked and mRNA decay is monitored over time . By systematically implementing these complementary approaches, researchers can definitively distinguish between transcriptional, post-transcriptional, and post-translational mechanisms controlling At1g47390 protein levels under their specific experimental conditions .

What are the considerations for using At1g47390 antibody in co-localization studies with confocal microscopy?

Implementing co-localization studies with At1g47390 antibody by confocal microscopy requires careful optimization of multiple parameters. Begin with fixation protocol optimization; aldehydes (2-4% paraformaldehyde) preserve cell architecture but may reduce epitope accessibility, while methanol enhances penetration but disrupts protein-protein interactions . Test different permeabilization conditions (0.1-0.5% Triton X-100, 0.05-0.2% Tween-20, or saponin) to balance antibody access with structural preservation. Antibody dilution requires careful titration (typically starting at 1:100-1:500) to maximize specific signal while minimizing background . For dual or triple labeling experiments with subcellular markers, select fluorophore combinations with minimal spectral overlap (e.g., Alexa 488/Cy3/Cy5) and implement sequential scanning to prevent bleed-through artifacts . Essential controls include: primary antibody omission, secondary antibody-only samples, single-label controls for multi-label experiments, pre-immune serum controls, and peptide competition controls with immunizing peptide. For co-localization with other proteins, prepare samples labeled with only one primary antibody to establish baseline signals and confirm secondary antibody specificity . Data analysis should include both qualitative assessment and quantitative co-localization metrics (Pearson's correlation coefficient, Manders' overlap coefficient) calculated from multiple cells and biological replicates. When interpreting results, remember that optical resolution limits (typically 200 nm laterally, 500 nm axially with standard confocal systems) may prevent distinction between true molecular interaction and proximity . Consider super-resolution techniques (STED, PALM, STORM) for more definitive co-localization at the molecular level. Finally, validate microscopy findings with biochemical approaches like co-immunoprecipitation or proximity ligation assays to confirm protein-protein interactions suggested by co-localization .

How can At1g47390 antibody be used to investigate protein degradation dynamics in response to environmental stresses?

Investigating At1g47390 protein degradation dynamics during stress responses requires specialized experimental designs leveraging antibody detection. Begin by establishing baseline degradation kinetics through cycloheximide chase assays under normal conditions; treat plants with cycloheximide (100-200 μg/mL) to block new protein synthesis, then harvest tissues at multiple timepoints (0, 1, 2, 4, 8, 12, 24 hours) for Western blotting with At1g47390 antibody to calculate protein half-life . To study stress effects, implement parallel cycloheximide chase assays under various stress conditions (drought, salt, cold, heat, oxidative stress, pathogen infection) and compare degradation curves. For mechanistic investigations, inhibit specific degradation pathways: MG132 (50 μM) for proteasome inhibition, E-64d (10 μM) for cysteine proteases, and 3-methyladenine (5 mM) for autophagy . Perform immunoprecipitation with At1g47390 antibody followed by ubiquitin immunoblotting to assess stress-induced changes in ubiquitination patterns. For spatial regulation, combine subcellular fractionation with quantitative immunoblotting to track stress-induced changes in At1g47390 localization that might affect degradation rates . To identify E3 ligases potentially regulating At1g47390 degradation during stress, perform co-immunoprecipitation with At1g47390 antibody followed by mass spectrometry under normal and stress conditions. For in vivo visualization of degradation dynamics, develop fluorescent timer fusion proteins with At1g47390 and validate their behavior against endogenous protein detected by antibody staining . Finally, correlate degradation patterns with physiological responses by measuring relevant stress response parameters (ROS production, stress-responsive gene expression, metabolite changes) in parallel with At1g47390 protein levels. This integrated approach reveals how At1g47390 protein stability regulation contributes to environmental stress adaptation in Arabidopsis .

How does At1g47390 antibody performance compare to antibodies against other F-box proteins in Arabidopsis?

Comparative analysis of At1g47390 antibody performance against other F-box protein antibodies reveals important technical considerations stemming from the unique characteristics of this protein family. The Arabidopsis genome encodes approximately 700 F-box proteins with varying expression levels, subcellular localizations, and structural features, creating diverse challenges for antibody development and application . At1g47390 antibody typically demonstrates moderate sensitivity (detection limit ~10-50 ng of recombinant protein) compared to antibodies against more abundant F-box proteins like TIR1 or COI1, which may detect <10 ng . Cross-reactivity profiles differ significantly based on sequence conservation; At1g47390 antibody shows minimal cross-reactivity with other F-box family members due to targeting of unique regions outside the conserved F-box domain, unlike some commercial antibodies that target conserved motifs and detect multiple family members . Regarding application versatility, At1g47390 antibody performs robustly in Western blotting and immunoprecipitation but may require additional optimization for immunohistochemistry compared to antibodies against more abundant F-box proteins . A critical difference emerges in detection of post-translational modifications; At1g47390 antibody effectively detects the unmodified protein but may have reduced affinity for ubiquitinated forms, requiring specialized extraction conditions and immunoprecipitation protocols to visualize these regulatory modifications . Finally, reproducibility across different plant growth stages varies; At1g47390 antibody provides consistent detection in vegetative tissues but may show reduced sensitivity in reproductive structures compared to antibodies against developmentally regulated F-box proteins with stage-specific expression patterns .

What are the key methodological differences when using At1g47390 antibody in different plant species beyond Arabidopsis?

Applying At1g47390 antibody across plant species requires methodological adaptations due to evolutionary divergence, tissue composition differences, and varying experimental challenges. First, epitope conservation must be assessed through sequence alignment of At1g47390 orthologues in target species; significant divergence (typically >30%) may necessitate new antibody development or epitope-targeted approaches . Protein extraction protocols require species-specific optimization; crop plants like rice or maize contain higher levels of interfering compounds requiring modified buffers with increased PVPP (4-6%), PVP (2-4%), and β-mercaptoethanol (10-20 mM) . Woody species like poplar need more stringent extraction conditions with higher detergent concentrations (2-3% Triton X-100) and mechanical disruption methods. Antibody working dilutions typically require re-optimization for cross-species applications, generally using more concentrated antibody (2-5 fold) than for Arabidopsis applications . Western blotting parameters need adjustment; transfer times should be extended for species with different protein composition, and membrane blocking requires optimization with species-specific non-reactive proteins to reduce background . Immunoprecipitation efficiency often decreases with evolutionary distance from Arabidopsis, requiring increased antibody amounts (3-5 μg vs. 1-2 μg for Arabidopsis) and extended incubation times (overnight vs. 4 hours) . Detection sensitivity varies dramatically across species; monocots typically show 40-60% reduced sensitivity compared to Arabidopsis due to greater cytoskeletal and cell wall interference. Finally, specificity verification becomes critical in cross-species applications; researchers should implement heterologous expression of the target species' orthologue with epitope tags for parallel detection, and use genomic tools (CRISPR, RNAi) in the target species to generate controls with reduced protein expression .

How can At1g47390 antibody be integrated with emerging technologies like proximity labeling or single-cell proteomics?

Integrating At1g47390 antibody with emerging technologies creates powerful approaches for understanding F-box protein biology at unprecedented resolution. For proximity labeling applications, At1g47390 antibody enables validation of BioID or TurboID fusion protein expression and localization before proximity labeling experiments . Researchers can create knock-in lines where endogenous At1g47390 is fused to promiscuous biotin ligases (BioID2, TurboID), verify correct expression using the antibody, then identify proximal proteins through streptavidin pulldown followed by mass spectrometry . This approach reveals the dynamic At1g47390 interactome under different conditions without artifacts from overexpression systems . For APEX2-based proximity labeling, At1g47390 antibody can verify fusion protein functionality through activity assays before implementing biotinylation protocols. In single-cell proteomics applications, At1g47390 antibody enables targeted protein detection in microfluidic platforms through antibody-based techniques like microwestern arrays or single-cell Western blotting . This allows correlation of At1g47390 levels with cellular phenotypes at single-cell resolution. For spatial proteomics, At1g47390 antibody can be combined with multiplexed ion beam imaging (MIBI) or CO-Detection by indEXing (CODEX) using metal-conjugated antibodies for simultaneous visualization of multiple proteins within intact plant tissues . At1g47390 antibody can also enhance CUT&Tag or CUT&RUN approaches for mapping chromatin associations with higher sensitivity than traditional ChIP methods, revealing indirect DNA associations mediated through protein interactions . For quantitative interactomics, At1g47390 antibody enables affinity purification combined with tandem mass tag (TMT) labeling for multiplexed comparison of interaction partners across conditions . Finally,At1g47390 antibody can validate results from nascent techniques like protein correlation profiling or thermal proteome profiling that reveal functional relationships through co-fractionation or thermal stability shifts, respectively .