RPS23 Antibody, HRP conjugated
Description
Fundamental Characteristics of RPS23 Antibody, HRP Conjugated
RPS23 Antibody, HRP conjugated is a rabbit polyclonal antibody specifically targeting the 40S ribosomal protein S23, with direct conjugation to Horseradish Peroxidase (HRP) . This specialized immunological reagent is designed for efficient detection of RPS23 in various experimental contexts, particularly in immunoassays such as ELISA (Enzyme-Linked Immunosorbent Assay) . The polyclonal nature of this antibody ensures recognition of multiple epitopes on the target protein, potentially enhancing detection sensitivity and robustness.
The direct conjugation with HRP offers significant practical advantages in laboratory settings. By eliminating the need for secondary antibody incubation steps, this conjugated antibody streamlines experimental protocols, reduces hands-on time, and minimizes potential sources of background or cross-reactivity. The HRP enzyme catalyzes the oxidation of substrates in the presence of hydrogen peroxide, generating detectable signals that can be measured through colorimetric, chemiluminescent, or fluorescent methods depending on the substrate used.
In the field of molecular biology and biochemistry, RPS23 Antibody, HRP conjugated serves as an essential tool for researchers investigating ribosomal structure and function, protein synthesis mechanisms, and translational regulation pathways. The ability to specifically detect RPS23, a critical component of the ribosomal machinery, contributes to our understanding of fundamental cellular processes and their dysregulation in pathological conditions.
The Target Protein: 40S Ribosomal Protein S23 (RPS23)
RPS23 is an integral component of the 40S ribosomal subunit, which, together with the 60S subunit, forms the complete 80S eukaryotic ribosome responsible for protein synthesis. This protein plays a critical role in the decoding process during translation, contributing to ribosomal structure and function.
Key characteristics of the RPS23 protein include:
RPS23 is highly conserved across species, suggesting its fundamental importance in cellular function and the evolutionary constraints on its structure. The high degree of conservation makes antibodies against RPS23 potentially cross-reactive with homologs from multiple species, although specific validation is necessary to confirm reactivity.
In terms of structure, RPS23 contributes to the decoding center of the ribosome, the site where mRNA codons are read during translation. Mutations in this protein can lead to defects in translation fidelity and protein synthesis. Research has implicated RPS23 in ribosomopathies, which are disorders characterized by ribosomal dysfunction . These conditions can manifest as developmental abnormalities, bone marrow failure, and increased cancer susceptibility, highlighting the critical nature of proper ribosomal function in cellular homeostasis.
Research Applications and Methodologies
The RPS23 Antibody, HRP conjugated has several important research applications, primarily centered around the detection and analysis of RPS23 protein in various biological contexts. The following applications represent the key areas where this antibody demonstrates utility:
Enzyme-Linked Immunosorbent Assay (ELISA)
ELISA represents the primary validated application for RPS23 Antibody, HRP conjugated . In this technique, the antibody can be used to detect and quantify RPS23 in biological samples such as cell lysates, tissue extracts, or serum. The direct HRP conjugation eliminates the need for secondary antibody incubation, streamlining the assay protocol and potentially reducing background signal.
The HRP conjugate produces a colorimetric signal when exposed to appropriate substrates, allowing for quantitative measurement of RPS23 levels through spectrophotometric methods. This application is particularly valuable for high-throughput screening or quantitative analysis of RPS23 expression across multiple samples.
Potential Applications in Western Blotting
While the HRP-conjugated version of the RPS23 antibody may not be specifically validated for Western blotting in the search results, similar antibodies against RPS23 have been demonstrated effective in this application . In Western blotting, the antibody can detect RPS23 (observed band size approximately 16 kDa) in protein samples separated by gel electrophoresis and transferred to a membrane.
Research has shown detection of RPS23 in various sample types, including:
The direct HRP conjugation could provide advantages in Western blotting by eliminating secondary antibody steps, although optimization would be necessary to ensure specific detection and minimal background.
Immunohistochemical Analysis
Immunohistochemical analysis using antibodies against RPS23 has been reported, allowing visualization of RPS23 expression patterns in tissue sections . In these applications, the antibody binds to RPS23 in fixed tissue samples, and the HRP conjugate catalyzes the conversion of substrates like DAB (3,3′-diaminobenzidine) to produce a visible stain.
For example, RPS23 antibodies have been used to examine expression in human liver cancer tissue sections, utilizing heat-mediated antigen retrieval with sodium citrate buffer (pH 6.0) and an HRP detection system . The direct HRP conjugation in the specific antibody being discussed could simplify such protocols by eliminating the secondary antibody incubation step.
Comparison with Other RPS23 Antibodies
The RPS23 Antibody, HRP conjugated represents one of several available antibody options for detecting and studying RPS23. Understanding the similarities and differences between these antibodies is essential for selecting the most appropriate reagent for specific research applications.
The key advantage of HRP-conjugated antibodies like the RPS23 Antibody, HRP conjugated is the direct detection capability, eliminating the need for secondary antibody incubation. This can reduce protocol complexity and duration, minimize background signal from secondary antibody cross-reactivity, and potentially enhance sensitivity through optimized enzyme-to-antibody ratios.
Different RPS23 antibodies target distinct regions of the protein, including N-terminal regions , middle segments (amino acids 44-143) , and full-length or recombinant protein-derived epitopes . This epitope diversity can be advantageous when specific protein domains must be detected, potential post-translational modifications must be avoided or targeted, or protein conformation affects epitope accessibility.
Research Significance and Applications in Molecular Biology
The availability of well-characterized antibodies against RPS23, including the HRP-conjugated variant, has significant implications for research in molecular biology, cell biology, and biomedical sciences. These applications include:
Studies of Ribosome Biogenesis and Function
The RPS23 Antibody, HRP conjugated enables investigation of ribosome assembly, maturation, and functional dynamics. By specifically detecting RPS23, researchers can monitor its incorporation into nascent 40S subunits, examine its expression levels under various cellular conditions, and assess its role in ribosomal complex formation.
Studies in yeast models have utilized RPS23 antibodies to investigate the consequences of RPS23 deficiency or mutation, including the GAL::RPS23A rps23bΔ yeast strain where one copy of the RPS23 gene is deleted and the other is under galactose-inducible control . Such research has revealed crucial insights into how alterations in RPS23 affect ribosomal function and cellular physiology.
Investigation of Ribosomopathies
Ribosomopathies are a class of disorders characterized by ribosomal dysfunction, often resulting from mutations in ribosomal proteins or factors involved in ribosome biogenesis. RPS23 has been implicated in certain ribosomopathies, and antibodies against this protein facilitate the study of these conditions at the molecular level .
The ability to detect RPS23 in patient samples, model organisms, or cell culture systems provides valuable tools for understanding the pathogenesis of these disorders and potentially developing therapeutic interventions. The HRP-conjugated antibody, with its direct detection capability, may offer advantages in diagnostic or screening applications.
Cancer Research and Cellular Stress Responses
Alterations in ribosomal protein expression and function have been associated with various cancers. The RPS23 Antibody, HRP conjugated can be employed to examine RPS23 expression in tumor samples, compare levels between normal and malignant tissues, and investigate potential correlations with disease progression or prognosis.
Additionally, cellular stress responses often involve modulation of protein synthesis machinery. The ability to monitor RPS23 levels and localization under stress conditions (such as nutrient deprivation, hypoxia, or exposure to toxins) can provide insights into how cells adapt their translational capacity in challenging environments.
Future Research Directions
The RPS23 Antibody, HRP conjugated has potential applications in several emerging research areas that could expand our understanding of ribosomal biology and related pathologies.
Expansion of Validated Applications
While currently validated primarily for ELISA , further characterization of the RPS23 Antibody, HRP conjugated could establish its utility in additional techniques such as immunocytochemistry for subcellular localization studies, flow cytometry for quantitative analysis in cell populations, and immunoprecipitation for protein-protein interaction studies. Each application would require specific optimization and validation protocols to ensure reliable performance.
Emerging Research Areas
Several cutting-edge research directions could benefit from well-characterized RPS23 antibodies, including:
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Specialized Ribosomes: Investigating the hypothesis that ribosomes with distinct protein compositions may preferentially translate specific mRNA subsets
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Ribosomal Response to Stress: Examining how cellular stressors affect RPS23 expression, modification, and incorporation into ribosomes
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Non-canonical Functions: Exploring potential extraribosomal roles of RPS23 in cellular processes beyond protein synthesis
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Therapeutic Targeting: Developing strategies to modulate ribosomal function in diseases associated with translational dysregulation
Future developments in antibody technology could enhance RPS23 detection through generation of highly specific monoclonal antibodies against defined RPS23 epitopes and development of recombinant antibodies with engineered properties for improved performance.
Product Specs
Components: 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
Ribosomal protein S23 (RPS23) is a component of the ribosome, a crucial ribonucleoprotein complex responsible for cellular protein synthesis. The small ribosomal subunit (SSU), which includes RPS23, binds messenger RNA (mRNA) and facilitates translation by selecting appropriate aminoacyl-transfer RNA (tRNA) molecules. The large ribosomal subunit (LSU) houses the peptidyl transferase center (PTC), the catalytic site responsible for peptide bond formation during polypeptide chain elongation. Nascent polypeptides exit the ribosome via a tunnel in the LSU, subsequently interacting with protein factors involved in post-translational modifications, targeting, and membrane insertion. RPS23 plays a significant role in maintaining translational fidelity.
- A missense mutation in RPS23 has been reported in two unrelated individuals presenting with microcephaly, hearing loss, and overlapping dysmorphic features. PMID: 28257692
- Studies have indicated dysregulated RPS23 expression in intervertebral disc degeneration. PMID: 25893343
- Research suggests that RPS23 hydroxylation can either enhance or diminish translational accuracy, depending on the stop codon context. PMID: 24550462
Q&A
What is RPS23 and why is it important in translational research?
RPS23, also known as small ribosomal subunit protein uS12, is a critical subunit of the 40S ribosome and serves as the first precursor of the small eukaryotic ribosomal subunit. Its significance stems from its strategic position in the decoding center of the ribosome, where it maintains translational fidelity by monitoring the complementarity between mRNA codons being translated and the anti-codons of aminoacyl-tRNAs. This quality control function is essential for accurate protein synthesis across eukaryotic organisms . Researchers target RPS23 to understand fundamental mechanisms of translational accuracy, ribosomal function, and their implications in various cellular processes and disease states .
What are the key characteristics of RPS23 antibodies used in research?
RPS23 antibodies are immunological tools designed to specifically recognize and bind to RPS23 protein. Key characteristics include:
| Feature | Specifications for RPS23 Antibody |
|---|---|
| Molecular Recognition | Targets 16 kDa RPS23 protein (observed MW: 16-18 kDa) |
| Host/Isotype | Typically Rabbit/IgG |
| Applications | Western Blot, ELISA |
| Reactivity | Human (may cross-react with other species) |
| Form | Liquid |
| Storage Requirements | Usually -20°C, stable for one year after shipment |
Most research-grade RPS23 antibodies are available in unconjugated form and require secondary detection systems, though HRP-conjugated versions offer direct detection capabilities for certain applications .
How does RPS23 hydroxylation affect ribosomal function?
RPS23 undergoes oxygen-dependent posttranslational modifications, specifically hydroxylation, which significantly impacts translational accuracy in an mRNA sequence-dependent manner. This modification affects stop codon readthrough, with studies showing that:
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Eukaryotic RPS23 hydroxylation is evolutionarily conserved across yeasts, flies, and humans
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Basal eukaryotes undergo two hydroxylations of RPS23, while animals typically exhibit only one hydroxylation
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Yeast ribosomes lacking hydroxylation show altered stop codon readthrough rates with differences up to ~10-fold
These findings demonstrate that oxygen-dependent modifications regulate translational accuracy and suggest potential approaches for modulating ribosomal fidelity in both research and therapeutic contexts .
What are the optimal dilutions and conditions for using RPS23 antibodies in Western Blot applications?
When using RPS23 antibodies for Western Blot applications, optimization is essential for specific detection and minimal background. The recommended dilution range is typically 1:5000-1:50000, though this should be titrated for each specific experimental system . Optimal conditions include:
| Application Parameter | Recommended Conditions |
|---|---|
| Dilution Range | 1:5000-1:50000 |
| Blocking Agent | 5% non-fat dry milk or BSA in TBST |
| Incubation Time | Primary: Overnight at 4°C Secondary: 1-2 hours at room temperature |
| Detection System | Standard ECL for unconjugated antibodies |
| Positive Controls | U2OS cells, A431 cells |
It's critical to note that sample-dependent variations may require adjustments to these parameters. Researchers should perform preliminary experiments with different dilutions to determine optimal conditions for their specific cell types and experimental setup .
How can researchers effectively employ RPS23 antibodies to study ribosomal assembly and function?
Researchers can employ RPS23 antibodies to investigate ribosomal assembly and function through several methodological approaches:
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Co-immunoprecipitation (Co-IP) studies: RPS23 antibodies can be used to pull down RPS23 and its interacting partners. This approach has successfully demonstrated interactions between endogenous OGFOD1 and uS12 proteins using standard immunoprecipitation protocols .
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Ribosomal profiling: Combining RPS23 antibodies with polysome profiling allows researchers to examine the incorporation of RPS23 into ribosomal subunits during assembly.
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Immunofluorescence microscopy: This approach helps visualize the subcellular localization of RPS23 during ribosome biogenesis.
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Functional assays combining genetics and biochemistry: Studies have used yeast strains with modified RPS23 genes (such as GAL::RPS23A rps23bΔ) alongside antibody-based detection to assess how mutations affect ribosome function .
For consistent results, researchers should include appropriate controls, such as normal rabbit immunoglobulin G, and validate findings using multiple complementary approaches to confirm specificity of detected interactions .
What methodological approaches can be used to study RPS23 hydroxylation and its impact on translation?
Studying RPS23 hydroxylation and its translational impact requires specialized methodological approaches:
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Mass spectrometry-based detection: High-resolution mass spectrometry using nanoLC Lumos platforms can detect RPS23 hydroxylation with stringent tolerances (m/z window ±5 ppm and 0.5 min retention time deviation) .
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Genetic manipulation systems: Creating yeast strains with controlled expression of RPS23 (GAL::RPS23A rps23bΔ) allows researchers to introduce wild-type or mutated versions of RPS23 and assess functional consequences .
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Stop codon readthrough assays: These assays measure how RPS23 hydroxylation affects translational accuracy by quantifying readthrough of premature stop codons in reporter constructs.
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Small molecule inhibition studies: Inhibitors targeting RPS23 hydroxylases have been shown to increase production of full-length proteins from sequences containing clinically relevant mutations, providing a tool to manipulate this pathway experimentally .
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Oxygen-dependent regulation analysis: Experiments conducted under varying oxygen conditions can reveal how hypoxia affects RPS23 modification and subsequent translational outcomes .
These approaches collectively provide a comprehensive framework for investigating how this oxygen-dependent post-translational modification regulates ribosomal function and protein synthesis accuracy.
What are common issues when using RPS23 antibodies and how can they be resolved?
Researchers working with RPS23 antibodies may encounter several technical challenges that can be addressed through strategic troubleshooting:
| Issue | Possible Causes | Troubleshooting Approaches |
|---|---|---|
| High background in Western blots | Insufficient blocking, antibody concentration too high | Increase blocking time/concentration, further dilute antibody (1:50000), use alternative blocking agents |
| Weak or no signal | Insufficient protein, degraded antibody, inefficient transfer | Increase protein loading, check antibody storage conditions, optimize transfer parameters |
| Multiple bands | Cross-reactivity, protein degradation, post-translational modifications | Use positive controls (U2OS, A431 cells), add protease inhibitors during sample preparation |
| Inconsistent results | Sample preparation variation, antibody lot differences | Standardize protocols, test antibody lots with positive controls |
When troubleshooting, it's advisable to run appropriate positive controls (such as U2OS or A431 cell lysates) that are known to express detectable levels of RPS23 protein . Additionally, incorporating loading controls (such as G6PDH antibody at 1:10,000 dilution) helps normalize for loading differences across samples .
How should researchers optimize storage and handling of RPS23 antibodies to maintain reactivity?
Proper storage and handling are crucial for maintaining RPS23 antibody reactivity and experimental reproducibility:
Following these guidelines ensures optimal antibody performance across experiments and maximizes shelf-life, particularly important when working with specialized antibodies like those targeting RPS23 .
What controls are essential when using RPS23 antibodies in various experimental applications?
Implementing appropriate controls is essential for experimental validity when using RPS23 antibodies:
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Positive controls: Include lysates from cell lines known to express RPS23, such as U2OS or A431 cells, to confirm antibody functionality .
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Negative controls:
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Loading controls: For Western blotting, include detection of housekeeping proteins such as G6PDH using anti-G6PDH antibodies (typical dilution 1:10,000) .
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Expression controls: When studying mutated versions of RPS23, include parallel experiments with wild-type RPS23 expression constructs to establish baseline comparisons .
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Antibody validation: Confirm antibody specificity through multiple techniques (Western blot, immunoprecipitation) or using genetic knockdown/knockout systems when possible.
These controls collectively help distinguish specific from non-specific interactions and provide essential benchmarks for data interpretation and troubleshooting .
How does RPS23 hydroxylation relate to disease mechanisms and potential therapeutic approaches?
RPS23 hydroxylation has significant implications for disease mechanisms and therapeutic development:
The posttranslational hydroxylation of RPS23 affects translational fidelity, particularly stop codon readthrough, which has direct relevance to several disease contexts:
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Genetic diseases with premature stop codons: Small-molecule inhibition of RPS23 hydroxylases has been shown to increase production of full-length proteins from sequences containing clinically relevant premature termination codons. This represents a potential therapeutic approach for diseases caused by nonsense mutations .
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Hypoxia-related pathologies: As RPS23 hydroxylation is oxygen-dependent, conditions involving hypoxia may exhibit altered ribosomal decoding accuracy. This connects RPS23 modification to cancer, ischemic diseases, and other pathologies characterized by low oxygen environments .
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Neurodegenerative diseases: The connection between RPS23-related genes and Alzheimer's disease pathologies suggests potential relevance to neurodegeneration. Research has shown that RPS23RG protein family members reduce AD-like pathologies (Aβ levels and tau phosphorylation) by interacting with adenylate cyclases to upregulate PKA activity and downregulate GSK-3 activity .
These findings point to potential therapeutic strategies targeting RPS23 hydroxylation to modulate ribosomal accuracy for medicinal applications, particularly for genetic diseases caused by premature termination codons .
What role does RPS23 play in the differentiation between human and mouse Alzheimer's disease susceptibility?
Research into RPS23-related genes has revealed intriguing connections to differential Alzheimer's disease susceptibility between humans and mice:
Studies have identified that retroposition of Rps23 mRNA occurred multiple times in different species but only generated two functionally expressed genes, Rps23rg1 and Rps23rg2, in mice . These genes encode proteins that appear to have protective effects against AD-like pathologies:
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The RPS23RG protein family members reduce Alzheimer's disease-like pathologies by:
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Importantly, while these functional Rps23rg genes exist in mice, extensive database searches found minimal evidence for functional homologs in humans, with only the rare ATG10 CRA_d isoform sharing limited homology to a dispensable domain of RPS23RG1 .
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This genomic difference may contribute to the observation that wild-type mice rarely develop AD-like pathologies while humans are more susceptible to Alzheimer's disease pathogenesis, characterized by Aβ overproduction/aggregation and tau hyperphosphorylation .
This research highlights how species-specific differences in the evolution of RPS23-derived genes may contribute to differential vulnerability to neurodegenerative disorders .
How can researchers investigate the functional consequences of RPS23 mutations on ribosomal decoding accuracy?
Investigating the functional consequences of RPS23 mutations on ribosomal decoding requires sophisticated experimental approaches:
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Yeast genetic systems: Researchers have developed specialized yeast strains (such as GAL::RPS23A rps23bΔ) where endogenous RPS23 expression can be controlled through galactose induction. These systems allow for complementation studies with plasmids expressing wild-type or mutated Rps23a proteins to assess functional consequences .
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Serial dilution growth assays: Growth comparisons between yeast expressing wild-type versus mutant RPS23 under selective conditions provide functional readouts of ribosomal fitness .
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Ribosomal profiling and accuracy assays: These techniques measure how RPS23 variants affect translation elongation rate, fidelity, and stop codon readthrough.
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Domain substitution experiments: Researchers have investigated the importance of specific RPS23 domains by creating chimeric proteins. For example, studies with RPS23RG family members demonstrated that substituting the transmembrane domain with that of other proteins (APP or nicastrin) abolished the interaction with adenylate cyclase 8 and eliminated downstream effects .
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Mass spectrometry analysis: High-resolution mass spectrometry with stringent tolerances (m/z window ±5 ppm and 0.5 min retention time deviation) enables detection of subtle modifications in RPS23 and their impact on ribosomal function .
These approaches collectively provide a framework for understanding how specific mutations in RPS23 affect the fundamental process of ribosomal decoding and translational accuracy .
What are the current research frontiers in understanding RPS23 post-translational modifications?
Current research on RPS23 post-translational modifications is expanding our understanding of translational regulation:
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Evolutionary conservation patterns: Studies have revealed that RPS23 hydroxylation is conserved across eukaryotes with interesting patterns: basal eukaryotes undergo two hydroxylations of RPS23, whereas animals typically exhibit only one hydroxylation. This evolutionary difference raises questions about functional specialization across taxonomic groups .
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Sequence-dependent effects: Recent findings indicate that RPS23 hydroxylation affects stop codon readthrough in an mRNA sequence-dependent manner, suggesting context-specific regulation of translational accuracy. Further research is investigating how sequence contexts surrounding stop codons interact with hydroxylated RPS23 .
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Oxygen-sensing mechanisms: The oxygen-dependent nature of RPS23 hydroxylation connects ribosomal function to cellular oxygen status. Active research is exploring how hypoxia affects this modification and subsequent translational outcomes, potentially linking environmental conditions to proteome regulation .
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Novel modification sites: Beyond known hydroxylation sites, researchers are using advanced mass spectrometry techniques with stringent tolerances to identify additional post-translational modifications of RPS23 and their functional significance .
These research directions are collectively expanding our understanding of how post-translational modifications fine-tune ribosomal function to meet cellular needs under different physiological conditions.
How do the structural features of RPS23 antibodies affect their experimental applications?
The structural features of RPS23 antibodies significantly influence their experimental utility:
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Antibody class and recombinant status: Recombinant antibodies like the RPS23 antibody (84560-1-RR) offer advantages of consistency and reproducibility compared to conventional polyclonal antibodies. The recombinant nature ensures batch-to-batch consistency, critical for longitudinal studies .
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Epitope recognition regions: Antibodies recognizing different epitopes of RPS23 may yield varying experimental outcomes. For instance, antibodies targeting the immunogen RPS23 fusion protein Ag31190 provide specific recognition patterns that may differ from those targeting other regions .
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Host species considerations: RPS23 antibodies raised in rabbits (IgG isotype) offer certain advantages for immunoprecipitation experiments due to protein A binding characteristics. This feature facilitates effective purification through protein A methods .
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Conjugation status: While unconjugated antibodies require secondary detection systems, directly conjugated antibodies (such as HRP-conjugated versions) enable direct detection, reducing experimental steps and potential sources of variability.
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Buffer composition effects: The storage buffer (PBS with 0.02% sodium azide and 50% glycerol, pH 7.3) preserves antibody stability but may influence certain applications. Researchers should consider buffer effects when designing experiments, particularly for applications sensitive to glycerol or sodium azide .
Understanding these structural features allows researchers to select appropriate antibodies for specific experimental applications and optimize protocols accordingly.
What are the most promising future directions for RPS23 research in translational medicine?
RPS23 research holds significant promise for translational medicine applications in several key areas:
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Therapeutic targeting of nonsense mutations: Small-molecule inhibition of RPS23 hydroxylases has demonstrated potential for increasing production of full-length proteins from sequences containing clinically relevant premature termination codons. This approach could lead to novel therapeutics for genetic diseases caused by nonsense mutations, potentially addressing thousands of currently untreatable conditions .
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Neurodegenerative disease interventions: The findings that RPS23RG family members can reduce Alzheimer's disease-like pathologies suggest potential therapeutic avenues. Though mice express functional Rps23rg genes while humans appear to lack direct homologs, understanding the downstream signaling mechanisms (involving adenylate cyclases, PKA activity, and GSK-3 regulation) could inform drug development for neurodegenerative conditions .
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Hypoxia-related disease management: The oxygen-dependent nature of RPS23 hydroxylation connects ribosomal function to cellular oxygen status, suggesting potential applications in hypoxia-related pathologies including cancer, stroke, and cardiovascular disease .
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Precision medicine approaches: The sequence-dependent effects of RPS23 modifications on translational accuracy suggest possibilities for targeted interventions based on specific genetic contexts, potentially enabling personalized treatment strategies for patients with specific mutation profiles .
