CRRSP54 Antibody

Shipped with Ice Packs
In Stock

Description

Search Methodology

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 .

Nomenclature Errors

  • 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  • Hypothetical Constructs: The term may refer to an unpublished or proprietary reagent not yet cataloged publicly .

Comparative Analysis of Similar Antibodies

While CRRSP54 is unverified, several structurally characterized antibodies targeting Arabidopsis thaliana proteins are documented in commercial databases (Table 1) :

Antibody NameTarget ProteinUniProt IDApplications
CSP41B AntibodyChloroplast stem-loop proteinQ9SA52Western Blot, ELISA
CP29B AntibodyChlorophyll-binding proteinQ9ZUU4Immunofluorescence
CYP19-4 AntibodyCytochrome P450 familyQ8LDP4Enzyme activity assays

These antibodies share features that CRRSP54 might hypothetically possess, such as:

  • Epitope Specificity: Defined using recombinant antigens .

  • Validation: Western Blot, ELISA, and immunohistochemistry .

Recommendations for Further Inquiry

  1. Verify Spelling: Confirm the correct identifier with original sources or collaborators.

  2. Explore Homologs: Investigate antibodies targeting proteins with similar domains (e.g., chloroplast-associated or cytochrome-related proteins) .

  3. Custom Synthesis: If CRRSP54 is a novel target, consider commissioning a custom antibody through vendors like Cusabio or R&D Systems .

Limitations of Current Data

The absence of CRRSP54 in indexed literature suggests it has not been:

  • Deposited in public repositories (GenBank, UniProt).

  • Commercially distributed as of March 2025 .

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.

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Composition: 50% Glycerol, 0.01M Phosphate Buffered Saline (PBS), pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
CRRSP54 antibody; At4g20530 antibody; F9F13.180Cysteine-rich repeat secretory protein 54 antibody
Target Names
CRRSP54
Uniprot No.

Target Background

Database Links
Protein Families
Cysteine-rich repeat secretory protein family
Subcellular Location
Secreted.

Q&A

What is CRRSP54 Antibody and what is its target protein?

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).

What are the optimal storage conditions for CRRSP54 Antibody?

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.

How should researchers validate CRRSP54 Antibody specificity?

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 .

What are the recommended dilutions for different experimental applications?

Optimal dilutions for CRRSP54 Antibody will vary based on the specific application:

ApplicationRecommended Dilution RangeIncubation ConditionsNotes
Western Blot1:500-1:20001-2 hours at RT or overnight at 4°CMay require optimization based on protein abundance
Immunohistochemistry1:100-1:5001-2 hours at RTFixation method may affect epitope accessibility
Immunofluorescence1:50-1:2001 hour at RTConsider using a signal amplification system for low-abundance targets
ELISA1:1000-1:5000According to protocolBSA or milk-based blocking agents recommended
Flow Cytometry1:50-1:20030-60 minutes on iceInclude 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.

How can researchers troubleshoot non-specific binding with CRRSP54 Antibody?

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.

What epitope targeting strategies were used in developing CRRSP54 Antibody?

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.

How can CRRSP54 Antibody be used in multiplex immunoassays?

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 .

What are the considerations for using CRRSP54 Antibody in tissue microarray analysis?

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.

How does clone selection affect CRRSP54 monoclonal antibody performance?

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.

How should researchers quantify and normalize CRRSP54 Antibody binding in comparative studies?

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 .

What controls should be included when using CRRSP54 Antibody in immunoprecipitation studies?

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 .

How can researchers address epitope masking when using CRRSP54 Antibody?

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.

How might CRRSP54 Antibody be integrated with emerging single-cell technologies?

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 .

What considerations are important for developing a phospho-specific version of CRRSP54 Antibody?

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.

How can computational modeling predict CRRSP54 Antibody cross-reactivity with related proteins?

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 .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2025 TheBiotek. All Rights Reserved.