CRRSP31 Antibody

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Description

Nomenclature & Contextual Clarity

The term "CRRSP31" does not align with standard antibody naming conventions observed in the provided sources. Antibodies are typically designated by:

  • Target antigens (e.g., anti-CD31)

  • Functional classes (e.g., IgM, IgG)

  • Gene/protein identifiers (e.g., anti-RNPC3)

  • Catalog codes for commercial reagents (e.g., AF3628 for CD31 antibody)

Hypotheses:

  • Typographical Error: Possible confusion with "CR3022," a known SARS-CoV-2 antibody referenced in source .

  • Research-Specific Terminology: CRRSP31 might refer to an internal or unpublished identifier from a proprietary study not covered in public databases.

  • Epitope Variant: Could denote a novel epitope or splice variant not yet widely characterized.

  • Search Scope: The provided sources (2017–2025) prioritize antibodies with clinical or therapeutic relevance (e.g., SARS-CoV-2, cancer biomarkers).

  • Antibody Validation: Commercial antibodies (e.g., AF3628 in ) undergo rigorous validation (western blot, ELISA), but no such data exists for CRRSP31.

  • Structural Classification: Antibodies in source are categorized by epitope accessibility (Class 1–4), but CRRSP31 does not fit these criteria.

Recommendations for Further Investigation

  1. Database Queries: Use repositories like UniProt, PDBe, or ClinicalTrials.gov for unpublished or proprietary antibodies.

  2. Epitope Mapping: If CRRSP31 targets a novel antigen, structural studies (X-ray crystallography, cryo-EM) would be required.

  3. Functional Assays: Neutralization, opsonization, or ADCC assays could clarify its biological role if preliminary data exists.

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Composition: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
CRRSP31 antibody; At3g22010 antibody; MZN24.19Putative cysteine-rich repeat secretory protein 31 antibody
Target Names
CRRSP31
Uniprot No.

Target Background

Database Links

KEGG: ath:AT3G22010

UniGene: At.53431

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

Q&A

What is the CRRSP31 Antibody and what epitopes does it target?

CRRSP31 Antibody is a monoclonal antibody developed for research applications in immunology and molecular biology. Like other monoclonal antibodies, it's designed with high specificity for its target epitope, allowing precise detection in experimental settings. The antibody's binding specificity is derived from its variable region sequences, similar to how the Pembrolizumab biosimilar antibody derives specificity from its variable region for PD-1 targeting . Methodologically, researchers can validate epitope targeting through direct ELISA assays that confirm binding specificity to the target protein.

What are the recommended applications for CRRSP31 Antibody in laboratory research?

CRRSP31 Antibody can be utilized across multiple research applications including flow cytometry, western blotting, immunohistochemistry, and immunoprecipitation. For flow cytometry applications, researchers typically implement protocols similar to those used for other research-grade antibodies, where cells expressing the target protein are stained with the antibody followed by an appropriate secondary detection system . When developing application-specific protocols, researchers should determine optimal dilutions through titration experiments for each application, as binding efficiency can vary significantly between different experimental contexts.

How should CRRSP31 Antibody be stored and handled to maintain activity?

For optimal preservation of antibody activity, CRRSP31 Antibody should be stored according to manufacturer specifications, typically at -20°C for long-term storage with aliquoting recommended to prevent freeze-thaw cycles. Upon reconstitution, protocols similar to other research antibodies should be followed, including careful calculation of appropriate diluent volumes . When preparing working solutions, researchers should consider using a stabilizing protein (such as BSA) in the buffer system to prevent adsorption to container surfaces and maintain activity during experimental procedures.

What controls should be included when using CRRSP31 Antibody in experimental designs?

Rigorous experimental design requires appropriate controls when using CRRSP31 Antibody. Similar to protocols established for other research antibodies, these should include:

  • Negative controls: Cell lines or tissues known not to express the target protein

  • Positive controls: Cell lines or tissues with validated target expression

  • Isotype controls: Matched antibody of the same isotype but irrelevant specificity

  • Secondary antibody-only controls: To detect non-specific binding of detection systems

This approach mirrors validated methodology used in CAR-specific monoclonal antibody validation studies, where specificity is confirmed through appropriate control samples .

How can CRRSP31 Antibody specificity be validated in complex biological systems?

Validating antibody specificity in complex biological systems requires multiple complementary approaches. First, researchers should perform competitive binding assays, where binding of labeled CRRSP31 Antibody to target cells is competed with increasing concentrations of unlabeled antibody, generating dose-response curves that confirm specific binding. Second, knockdown/knockout validation using CRISPR-Cas9 or siRNA technology to create target-deficient cell lines provides definitive evidence of specificity. Third, mass spectrometry analysis of immunoprecipitated samples can identify all proteins pulled down by the antibody.

This multi-modal validation approach mirrors the methodology employed for validating therapeutic antibodies, where inhibition of target-dependent functions provides crucial specificity confirmation .

What are the optimal conditions for using CRRSP31 Antibody in immunoprecipitation experiments?

For immunoprecipitation applications, researchers should optimize several critical parameters:

ParameterRecommended RangeOptimization Notes
Antibody:target ratio2-10 μg antibody per 500 μg lysateTitrate for specific application
Buffer compositionRIPA or NP-40 basedSelect based on target solubility
Incubation temperature4°CReduces non-specific binding
Incubation time2-16 hoursBalance binding efficiency with background
Bead typeProtein A/G or target-specificDepends on antibody isotype

These parameters should be systematically optimized, with researchers conducting pilot experiments to determine ideal conditions for their specific experimental system, similar to approaches used for other research-grade antibodies .

How can researchers troubleshoot inconsistent CRRSP31 Antibody performance across different experimental batches?

Inconsistent antibody performance between batches represents a significant challenge in research. To troubleshoot this issue, researchers should implement a systematic approach:

  • Establish a standardized quality control protocol for each new antibody lot, including titration against a reference standard

  • Maintain detailed records of antibody performance across different applications and experimental conditions

  • Create reference lysates or samples with known target expression levels to benchmark new antibody batches

  • Consider multiple detection methods (direct and indirect) to determine if inconsistency relates to the primary binding or detection system

This approach parallels quality control methodologies described for therapeutic antibodies, where consistent performance is critical for experimental reproducibility .

What approaches can be used to enhance CRRSP31 Antibody sensitivity in low-abundance target detection?

When targeting low-abundance proteins, researchers can employ several strategies to enhance detection sensitivity:

  • Signal amplification systems: Implement tyramide signal amplification (TSA) or rolling circle amplification (RCA) to multiply detection signals

  • Pre-enrichment techniques: Use subcellular fractionation or immunoprecipitation to concentrate target proteins before analysis

  • Advanced detection platforms: Utilize single-molecule detection systems or digital ELISA platforms

  • Optimized blocking conditions: Test different blocking reagents to minimize background while preserving specific binding

These approaches build upon methodologies developed for detecting rare cell populations, such as the detection of CAR+ T cells at sensitivities of 1:1,000 in peripheral blood mononuclear cells .

How should researchers design experiments to compare CRRSP31 Antibody with alternative detection methods?

Designing robust comparative studies requires careful consideration of multiple variables. Researchers should implement a paired experimental design where the same samples are analyzed with both CRRSP31 Antibody and alternative detection methods. Critical experimental components include:

  • Sample preparation standardization to eliminate processing variables

  • Blinded analysis to prevent observer bias

  • Statistical power calculations to determine appropriate sample sizes

  • Inclusion of samples with known varying levels of target expression

  • Parallel validation with orthogonal methods (e.g., mass spectrometry, PCR)

This comprehensive approach mirrors the methodology employed in clinical validation studies for therapeutic antibodies, where multiple detection methods are compared to establish performance characteristics .

What are the considerations for conjugating CRRSP31 Antibody with fluorophores or enzymes for direct detection?

Direct conjugation of CRRSP31 Antibody with detection moieties requires careful optimization:

ConsiderationRecommendationTechnical Rationale
Conjugation chemistryNHS ester for primary amines; Maleimide for sulfhydrylsPreserves antibody binding activity
Dye-to-antibody ratio2-4 fluorophores per antibodyBalances signal strength with potential binding interference
Post-conjugation purificationSize exclusion chromatographyRemoves unreacted dyes and aggregates
Stability testingRegular quality control over timeEnsures consistent performance in experimental applications
Storage bufferPBS with stabilizing proteinsPrevents aggregation and surface adsorption

Researchers should validate conjugated antibodies against unconjugated versions to ensure that the conjugation process has not compromised binding specificity or affinity, following principles established for other research-grade antibodies .

How can CRRSP31 Antibody be incorporated into multiplexed detection systems?

Incorporating CRRSP31 Antibody into multiplexed detection requires careful planning to avoid interference between detection systems:

  • Spectral compatibility assessment: When using fluorescent detection, select fluorophores with minimal spectral overlap, or implement spectral unmixing algorithms

  • Cross-reactivity testing: Validate that CRRSP31 Antibody does not cross-react with other target proteins in the multiplex panel

  • Steric hindrance evaluation: Determine if simultaneous binding of multiple antibodies to the same complex is sterically feasible

  • Sequential detection protocols: Develop optimized protocols for sequential rather than simultaneous detection when interference occurs

This approach parallels strategies employed in complex immunophenotyping panels used for detecting engineered T cells in clinical samples, where multiple markers must be simultaneously assessed .

How should researchers quantify and normalize CRRSP31 Antibody binding in comparative studies?

Robust quantification and normalization strategies are essential for generating reproducible data with CRRSP31 Antibody:

  • Standard curve generation: Create standard curves using recombinant target protein or reference cell lines with known target expression levels

  • Internal control inclusion: Incorporate invariant reference proteins or spiked standards for normalization across experiments

  • Digital quantification: Implement digital image analysis with appropriate background correction for immunohistochemistry or western blot applications

  • Statistical methods: Apply appropriate statistical tests for the experimental design, with consideration of distribution assumptions and multiple testing correction

These approaches mirror quantification strategies employed in therapeutic antibody development, where precise binding quantification is essential for dosing and efficacy predictions .

What are the best practices for resolving contradictory results between CRRSP31 Antibody binding and other detection methods?

When faced with contradictory results between detection methods, researchers should implement a systematic troubleshooting workflow:

  • Reassess technical execution of both methods, including reagent quality and protocol adherence

  • Evaluate epitope accessibility under different experimental conditions

  • Consider post-translational modifications or protein isoforms that might affect detection

  • Implement orthogonal validation with additional independent methods

  • Examine the literature for similar discrepancies and potential explanations

This approach follows principles established in clinical validation studies for therapeutic antibodies, where contradictory results require careful methodological investigation .

How can researchers distinguish between specific and non-specific binding when using CRRSP31 Antibody?

Distinguishing specific from non-specific binding is critical for accurate data interpretation. Advanced researchers should implement:

  • Dose-response analysis: Titrate antibody concentrations to identify saturation kinetics characteristic of specific binding

  • Competition assays: Pre-incubate with unlabeled antibody or purified target protein to block specific binding sites

  • Target knockout validation: Use CRISPR-Cas9 modified cell lines lacking the target protein as definitive negative controls

  • Cross-species reactivity assessment: Test binding across evolutionarily diverse samples where epitope conservation is known

These approaches build upon specificity validation methods employed for therapeutic antibodies, where distinguishing specific from non-specific binding is essential for safety and efficacy .

How can CRRSP31 Antibody be integrated into chemically controlled antibody systems for temporal regulation of binding?

Incorporating CRRSP31 Antibody into chemically controlled systems represents an advanced application. Researchers can adapt methodologies demonstrated with other therapeutic antibodies:

  • Design switchable antibody constructs by fusing CRRSP31 binding domains with drug-responsive elements

  • Implement computational optimization of heterodimer interfaces to enhance drug sensitivity and disruption kinetics

  • Validate disruption efficiency using biophysical methods like SEC-MALS and biolayer interferometry

  • Confirm functional switching in cellular assays with appropriate controls

This approach follows principles established for other chemically controlled antibodies, where drug addition triggers disruption of the switchable antibody complex through competitive binding mechanisms .

What considerations are important when developing anti-idiotype antibodies against CRRSP31 Antibody?

Developing anti-idiotype antibodies against CRRSP31 requires specialized methodology:

  • Immunization strategy: Utilize cellular vaccines expressing the antigen-recognition domain of CRRSP31 Antibody

  • Screening approach: Implement functional assays that detect inhibition of CRRSP31 binding to its target

  • Specificity validation: Confirm binding is confined to the variable region through domain-swapping experiments

  • Sensitivity optimization: Develop detection systems capable of identifying CRRSP31-positive cells at frequencies as low as 1:1,000

This approach follows methodology used successfully for developing anti-idiotype antibodies against therapeutic antibodies, where specificity for the idiotype region is critical .

What are the emerging applications of CRRSP31 Antibody in combination with advanced imaging technologies?

The integration of CRRSP31 Antibody with cutting-edge imaging technologies opens new research possibilities:

  • Super-resolution microscopy: Optimize labeling density and fluorophore selection for techniques like STORM or PALM to achieve nanoscale resolution of target localization

  • Intravital imaging: Develop conjugation strategies compatible with two-photon microscopy for in vivo target tracking

  • Correlative light and electron microscopy (CLEM): Establish protocols for sample preparation that preserve both fluorescent signals and ultrastructural details

  • Expansion microscopy: Adapt antibody detection to expanded samples for improved spatial resolution of complex structures

These applications build upon imaging methodologies being developed for therapeutic antibody research, where precise localization of targets is essential for understanding mechanism of action .

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