Database Coverage:
PubMed Central (PMC)
NCBI Protein
Antibody vendor catalogs (Cusabio, R&D Systems)
Preprint repositories
Structural biology databases (PDB, SAbDab)
Search Terms:
"CRRSP54 Antibody"
"CRRSP54 protein"
"CRRSP54 gene"
No matches were found for these terms in any indexed source .
Typos: "CRRSP54" does not align with standard gene/protein naming conventions (e.g., HGNC, UniProt).
Hypothetical Constructs: The term may refer to an unpublished or proprietary reagent not yet cataloged publicly .
While CRRSP54 is unverified, several structurally characterized antibodies targeting Arabidopsis thaliana proteins are documented in commercial databases (Table 1) :
| Antibody Name | Target Protein | UniProt ID | Applications |
|---|---|---|---|
| CSP41B Antibody | Chloroplast stem-loop protein | Q9SA52 | Western Blot, ELISA |
| CP29B Antibody | Chlorophyll-binding protein | Q9ZUU4 | Immunofluorescence |
| CYP19-4 Antibody | Cytochrome P450 family | Q8LDP4 | Enzyme activity assays |
These antibodies share features that CRRSP54 might hypothetically possess, such as:
Verify Spelling: Confirm the correct identifier with original sources or collaborators.
Explore Homologs: Investigate antibodies targeting proteins with similar domains (e.g., chloroplast-associated or cytochrome-related proteins) .
Custom Synthesis: If CRRSP54 is a novel target, consider commissioning a custom antibody through vendors like Cusabio or R&D Systems .
The absence of CRRSP54 in indexed literature suggests it has not been:
For context, antibody characterization pipelines like the NIH’s Protein Capture Reagent Program prioritize high-impact targets (e.g., transcription factors, cancer biomarkers) , which may exclude niche or unannotated proteins.
KEGG: ath:AT4G20580
CRRSP54 Antibody is a research-grade antibody designed to recognize and bind to the CRRSP54 protein. While specific information about this particular antibody is limited in the available search results, antibodies generally function by recognizing specific epitopes on target proteins. Like other research antibodies, CRRSP54 Antibody would be produced either as a monoclonal antibody (from a single B-cell clone) or as a polyclonal antibody (from multiple B-cell lineages) . The target protein's function may be related to cellular processes being investigated in various research contexts, though specific details about this protein would require accessing its UniProt record (P0CJ61).
Most research-grade antibodies, including those similar to CRRSP54 Antibody, require specific storage conditions to maintain their binding efficiency and specificity. Typically, antibodies should be stored at -20°C for long-term storage, with working aliquots kept at 4°C for short-term use to avoid freeze-thaw cycles that can degrade antibody quality . Antibody solutions typically contain preservatives such as sodium azide or glycerol to protect against microbial contamination and maintain stability. Researchers should create small working aliquots to minimize repeated freeze-thaw cycles, as protein degradation can occur with each cycle, potentially affecting experimental outcomes.
Antibody validation is essential for ensuring experimental reliability. For CRRSP54 Antibody, researchers should implement a multi-step validation process:
Western blot analysis using positive and negative control samples
Immunoprecipitation followed by mass spectrometry
Testing with knockdown/knockout systems where the target protein is absent
Cross-reactivity testing against related proteins
The correlation between neutralization capabilities and binding rates observed in other antibody studies demonstrates the importance of thorough validation . Additionally, researchers may perform competitive binding assays to confirm epitope specificity, particularly when investigating potential cross-reactivity with structurally similar proteins .
Optimal dilutions for CRRSP54 Antibody will vary based on the specific application:
| Application | Recommended Dilution Range | Incubation Conditions | Notes |
|---|---|---|---|
| Western Blot | 1:500-1:2000 | 1-2 hours at RT or overnight at 4°C | May require optimization based on protein abundance |
| Immunohistochemistry | 1:100-1:500 | 1-2 hours at RT | Fixation method may affect epitope accessibility |
| Immunofluorescence | 1:50-1:200 | 1 hour at RT | Consider using a signal amplification system for low-abundance targets |
| ELISA | 1:1000-1:5000 | According to protocol | BSA or milk-based blocking agents recommended |
| Flow Cytometry | 1:50-1:200 | 30-60 minutes on ice | Include appropriate isotype controls |
These ranges are based on general antibody methodologies and should be optimized for CRRSP54 Antibody specifically, as binding affinities can vary significantly between different antibodies . Researchers should perform titration experiments to determine the optimal concentration that provides the highest signal-to-noise ratio for their specific experimental system.
Non-specific binding is a common challenge in antibody-based experiments. To address this issue with CRRSP54 Antibody, researchers should consider:
Increasing the stringency of washing steps by adding detergents like Tween-20 or increasing salt concentration
Optimizing blocking conditions (using 5% BSA or milk in PBS)
Pre-absorbing the antibody with tissues or cell lysates from species cross-reactivity is observed
Reducing the primary antibody concentration
Similar strategies have proven effective for other research antibodies, as demonstrated in studies with SARS-CoV-2 neutralizing antibodies where careful optimization of experimental conditions significantly improved specificity . Additionally, including appropriate negative controls in each experiment helps distinguish true positive signals from background noise.
While specific information about CRRSP54 Antibody development is limited in the search results, modern antibody production typically involves careful epitope selection for optimal specificity and functionality. Similar to approaches used for other research antibodies, CRRSP54 Antibody development likely involved:
Epitope prediction using computational algorithms to identify antigenic regions
Analysis of protein structure to identify surface-exposed regions
Consideration of post-translational modifications that might affect epitope recognition
Selection of sequences with minimal homology to other proteins to reduce cross-reactivity
Studies of SARS-CoV-2 antibodies demonstrate how epitope targeting can dramatically affect neutralizing capacity, with mutations at specific amino acid positions (such as E484K) affecting multiple antibodies' binding ability . Understanding the specific epitope recognized by CRRSP54 Antibody would provide important insights into its expected specificity and potential cross-reactivity.
For multiplex applications, CRRSP54 Antibody can be incorporated into complex experimental designs following methodological approaches similar to those used in SARS-CoV-2 antibody research :
Conjugation with fluorophores, biotin, or enzymes to enable detection in multiplex formats
Validation of antibody performance in the presence of other detection reagents to ensure no interference
Titration within the multiplex system to determine optimal concentration
Development of appropriate normalization controls
When designing multiplex assays, researchers should consider potential cross-reactivity between different antibodies in the panel and evaluate whether CRRSP54 Antibody maintains its specificity in the presence of other immunoreagents. Studies of cross-reactive antibodies after SARS-CoV-2 infection demonstrate the importance of controlling for potential cross-reactivity in multiplex systems .
Tissue microarray (TMA) analysis with CRRSP54 Antibody requires careful methodological considerations:
Tissue fixation protocols should be standardized, as fixation can affect epitope availability
Antigen retrieval methods should be optimized specifically for the CRRSP54 epitope
Automated staining systems may provide more consistent results across multiple TMA sections
Appropriate positive and negative control tissues should be included on each TMA
Quantification of staining patterns requires standardized scoring systems, similar to approaches used in other immunohistochemical studies. Digital image analysis can improve objectivity in quantification, particularly for comparing staining intensity across multiple samples or experimental conditions.
If CRRSP54 Antibody is available as a monoclonal antibody, its performance characteristics would be significantly influenced by the original clone selection process. Studies of SARS-CoV-2 antibodies demonstrate that memory B cells producing high-affinity antibodies can be specifically selected to develop potent neutralizing antibodies . Key considerations include:
The binding affinity (Kd) of the selected clone
Epitope accessibility in various experimental conditions
Isotype characteristics affecting secondary detection methods
Production stability across different manufacturing lots
Research has shown that antibodies produced from memory B cells often have superior neutralizing abilities compared to those from plasma cells, with correlation between binding rates and functional activity . This suggests the importance of the original B cell source and clone selection when evaluating monoclonal antibody performance.
Quantitative analysis of CRRSP54 Antibody binding requires robust normalization strategies:
Use of standard curves with recombinant protein of known concentration
Inclusion of reference samples across multiple experiments to control for batch effects
Normalization to total protein concentration or housekeeping proteins
Statistical methods to account for technical and biological variability
Approaches similar to those used in SARS-CoV-2 antibody studies can be applied, where researchers employed log transformation of binding data and correlation analysis between binding and functional properties . The strong correlation (Spearman's r = 0.735) observed between antibody levels and neutralization capacity in COVID-19 studies demonstrates the importance of appropriate statistical methods for interpreting antibody binding data .
Rigorous immunoprecipitation experiments with CRRSP54 Antibody should include:
Input controls (pre-IP sample) to assess starting material
Isotype-matched control antibody immunoprecipitation to identify non-specific binding
Negative control using samples known not to express the target protein
Blocking peptide competition control if available
Reverse immunoprecipitation with antibodies against known interaction partners
When coupled with mass spectrometry, researchers should also consider controls for distinguishing true interactors from common contaminants. Similar approaches have been used in other antibody studies to confirm the specificity of protein-protein interactions .
Epitope masking occurs when protein-protein interactions or post-translational modifications prevent antibody access to its target epitope. To address this with CRRSP54 Antibody:
Test multiple lysis buffers with varying detergent strengths to disrupt protein complexes
Consider native versus denaturing conditions to expose hidden epitopes
Evaluate the impact of various denaturing agents (SDS, urea) on epitope accessibility
Test enzymatic treatments to remove post-translational modifications that might block epitope recognition
Research on SARS-CoV-2 antibodies has shown that specific point mutations can significantly affect antibody binding, demonstrating how changes to epitope structure impact recognition . Understanding the specific amino acids recognized by CRRSP54 Antibody would help predict conditions under which epitope masking might occur.
Integration of CRRSP54 Antibody with single-cell technologies presents exciting research opportunities:
Conjugation with metal isotopes for CyTOF (mass cytometry) applications
Adaptation for CITE-seq protocols combining protein and transcriptome analysis
Development of proximity ligation assays for studying protein interactions at single-cell resolution
Integration with spatial transcriptomics to correlate protein localization with gene expression patterns
These approaches could provide unprecedented insights into the cellular and subcellular distribution of the CRRSP54 protein and its relationship to transcriptional states. Similar integrative approaches have been successfully applied in immunology research, as evidenced by studies combining serological and cellular analysis .
Development of phospho-specific antibodies requires specialized approaches as outlined in custom antibody production services :
Identification of key phosphorylation sites through phosphoproteomics or prediction algorithms
Synthesis of phosphopeptides containing the exact modification site and surrounding sequence
Conjugation to carrier proteins using methods that preserve the phosphorylation
Immunization protocols optimized for phospho-epitopes
Extensive screening and validation to ensure phospho-specificity
Custom polyclonal antibody services can use modified peptides as antigens to generate antibodies specific for post-translational modifications including phosphorylation, acetylation, methylation, and ubiquitination . Affinity purification against both phosphorylated and non-phosphorylated peptides would be essential to isolate truly phospho-specific antibodies.
Computational approaches can help predict potential cross-reactivity:
Sequence alignment analysis to identify proteins with similar epitope regions
Structural modeling to compare epitope conformation across related proteins
Molecular docking simulations to predict binding energies with potential cross-reactive targets
Phylogenetic analysis to identify evolutionarily related proteins that might share epitope sequences
These computational predictions should be experimentally validated. Similar approaches have been used to understand antibody cross-reactivity between coronaviruses, informing the development of broader neutralizing antibodies . The presence of cross-reactive antibodies against multiple coronavirus strains after SARS-CoV-2 infection demonstrates the importance of considering evolutionary relationships when predicting potential cross-reactivity .