NXPH2 Antibody

What is NXPH2 and why is it important in neuroscience research?

NXPH2 (Neurexophilin-2) is a secreted protein belonging to the neurexophilin family. It functions as a signaling molecule that resembles neuropeptides and acts by binding to alpha-neurexins and possibly other receptors . NXPH2 is primarily expressed in brain and kidney tissues , making it relevant for neuroscience research investigating synaptic function and neuronal signaling pathways.

The importance of NXPH2 in neuroscience stems from its potential role in modulating synaptic transmission through its interaction with neurexins, which are key synaptic adhesion molecules. Researching NXPH2 can provide insights into neural circuit formation, synaptic plasticity, and potentially neurological disorders associated with synaptic dysfunction.

What are the key structural features and post-translational modifications of NXPH2?

NXPH2 is a relatively small protein with a calculated molecular weight of approximately 30 kDa . The protein contains several key structural features:

• A signal peptide for secretion

• An N-terminal non-conserved domain

• A central conserved domain characteristic of the neurexophilin family

Notable post-translational modifications of NXPH2 include:

NXPH2 undergoes proteolytic processing at the boundary between the N-terminal non-conserved domain and the central conserved domain, particularly in neuron-like cells . This processing is likely important for its biological function.

How do researchers distinguish between NXPH2 and the related NXPE2 protein?

Distinguishing between NXPH2 (Neurexophilin-2) and NXPE2 (Neurexophilin and PC-esterase domain family member 2) requires attention to several key differences:

• Molecular Weight: NXPH2 has a molecular weight of approximately 30 kDa , while NXPE2 is significantly larger at 64.9 kDa with 559 amino acid residues .

• Subcellular Localization: NXPH2 is primarily a secreted protein , whereas NXPE2 is localized to the membrane .

• Tissue Expression Pattern: While NXPH2 is predominantly expressed in brain and kidney , NXPE2 shows notable expression in salivary gland, epididymis, colon, and appendix .

• Antibody Validation: When using antibodies, researchers should verify target specificity through techniques such as Western blotting at the expected molecular weight, using appropriate positive and negative controls, and confirming the expression pattern matches known tissue distribution.

• Domain Structure: The proteins belong to different families despite similarity in naming, with NXPE2 containing a PC-esterase domain not present in NXPH2.

What are the optimal experimental conditions for Western blot detection of NXPH2?

Optimizing Western blot conditions for NXPH2 detection requires careful consideration of several parameters:

• Sample Preparation:

  • Use tissues with known NXPH2 expression (brain or kidney) as positive controls

  • For cell lines, HEK293T cells and neuronal cell lines are suitable

  • Ensure complete lysis with appropriate buffers containing protease inhibitors

  • Include phosphatase inhibitors if studying phosphorylated forms of NXPH2

• Antibody Selection and Dilution:

  • For commercial antibodies, dilution ratios typically range from 1:500-1:2000

  • Polyclonal antibodies may provide better sensitivity for detecting native NXPH2

  • Consider using antibodies targeting different epitopes for validation

• Electrophoresis and Transfer Conditions:

  • Use SDS-PAGE gels with appropriate concentration (10-12% recommended)

  • Run at 29-30 kDa marker region for the main NXPH2 band

  • Consider wet transfer systems for optimal protein transfer

• Blocking and Detection:

  • 5% non-fat milk or BSA in TBST is typically sufficient for blocking

  • Incubate primary antibody at 4°C overnight for optimal binding

  • HRP-conjugated secondary antibodies with compatible chemiluminescent detection systems provide good sensitivity

• Controls and Validation:

  • Include both positive (brain/kidney tissue lysates) and negative controls

  • Consider using recombinant NXPH2 as a standard

Expected results should show a distinct band at approximately 30 kDa, though additional bands may appear if detecting proteolytically processed forms of the protein.

How should researchers optimize immunohistochemistry protocols for NXPH2 detection in brain tissues?

Optimizing immunohistochemistry (IHC) for NXPH2 detection in brain tissues requires attention to several critical parameters:

• Tissue Preparation:

  • For IHC-P: Use 4% paraformaldehyde fixation (4-24 hours depending on tissue size)

  • For IHC-F: Snap-freeze tissue in OCT compound and prepare 10-20 μm sections

  • Consider antigen retrieval methods (citrate buffer pH 6.0 or EDTA buffer pH 9.0) for formalin-fixed tissues

• Antibody Selection and Dilution:

  • Start with recommended dilutions (typically 1:50-1:200 for IHC applications)

  • Consider using fluorophore-conjugated primary antibodies (like AbBy Fluor® 555) for direct detection

  • If using unconjugated primary antibodies, select species-appropriate secondary antibodies

• Protocol Optimization:

  • Extended blocking (1-2 hours) with 5-10% normal serum from the same species as the secondary antibody

  • Optimize primary antibody incubation time (overnight at 4°C often yields best results)

  • Include 0.1-0.3% Triton X-100 in buffers to enhance antibody penetration for neuron-specific staining

• Controls and Validation:

  • Positive controls: Human or mouse brain sections (regions with known NXPH2 expression)

  • Negative controls: Omission of primary antibody and tissues with minimal NXPH2 expression

  • Consider co-staining with neuronal markers to confirm cell-type specificity

• Signal Enhancement and Background Reduction:

  • Tyramide signal amplification for low-abundance targets

  • Autofluorescence quenching for brain tissues (Sudan Black B treatment)

  • Careful washing steps (at least 3×10 minutes) after antibody incubations

Expected results should show predominantly neuronal staining patterns in brain tissues with potential secretory patterns consistent with NXPH2's role as a secreted protein.

What considerations are important when selecting between polyclonal and monoclonal NXPH2 antibodies?

The selection between polyclonal and monoclonal NXPH2 antibodies should be guided by experimental requirements and research objectives:

Polyclonal NXPH2 Antibodies:

• Advantages:

  • Recognize multiple epitopes, potentially increasing detection sensitivity

  • Better tolerance for protein denaturation or conformational changes

  • Generally less expensive and easier to produce

  • May detect various isoforms or post-translationally modified variants

• Best Applications:

  • Western blotting for maximal sensitivity

  • Initial protein characterization studies

  • Detection of low-abundance proteins

  • Applications where protein conformation may be altered

• Limitations:

  • Batch-to-batch variability requiring validation across lots

  • Potential for cross-reactivity with related proteins

  • Less specificity for distinguishing highly similar proteins

Monoclonal NXPH2 Antibodies:

• Advantages:

  • Consistent specificity across experiments and batches

  • Reduced background and non-specific binding

  • Superior for distinguishing between closely related proteins

  • Better for quantitative applications

• Best Applications:

  • Experiments requiring high reproducibility

  • Flow cytometry and immunoprecipitation

  • Therapeutic and diagnostic applications

  • Long-term studies requiring consistent reagents

• Limitations:

  • May recognize only a single epitope, reducing detection if that epitope is masked

  • Sometimes less sensitive than polyclonal antibodies

  • More susceptible to epitope loss through fixation or denaturation

  • Generally more expensive

Decision Framework:

• For discovery-phase research, polyclonal antibodies may provide better detection

• For specific quantitative assays or advanced applications, monoclonal antibodies offer greater consistency

• Consider using both types for validation and confirmation of findings

How can researchers address non-specific binding or high background issues when using NXPH2 antibodies?

Non-specific binding and high background are common challenges when working with NXPH2 antibodies. These methodological approaches can help address these issues:

• Antibody Dilution Optimization:

  • Perform a dilution series (e.g., 1:100, 1:500, 1:1000, 1:5000) to identify optimal concentration

  • Higher dilutions typically reduce background but may compromise specific signal intensity

  • Document signal-to-noise ratio at each dilution to determine optimal working concentration

• Blocking Optimization:

  • Test different blocking reagents (BSA, normal serum, commercial blocking buffers)

  • Extend blocking time to 1-2 hours at room temperature

  • Consider adding 0.1-0.5% Tween-20 to blocking buffer to reduce hydrophobic interactions

  • For tissue sections, include avidin/biotin blocking steps if using biotinylated detection systems

• Washing Procedures:

  • Increase washing duration (3-5 washes of 5-10 minutes each)

  • Use gentle agitation during washing steps

  • Consider adding higher salt concentration (up to 500 mM NaCl) to wash buffer for reducing ionic interactions

• Secondary Antibody Considerations:

  • Pre-adsorb secondary antibodies against tissue powder

  • Use secondary antibodies specifically cross-adsorbed against other species

  • Reduce secondary antibody concentration

• Sample-Specific Approaches:

  • For Western blot: Use freshly prepared samples and PVDF membranes (better for protein binding)

  • For IHC: Optimize fixation time and antigen retrieval methods

  • For ICC: Test different fixation protocols (4% PFA vs. methanol)

• Controls to Include:

  • No primary antibody control to assess secondary antibody background

  • Isotype control to evaluate non-specific binding

  • Pre-absorption with immunizing peptide to confirm specificity

If high background persists, consider switching to a different NXPH2 antibody targeting an alternative epitope or from a different manufacturer.

What strategies can be employed when NXPH2 antibodies show unexpected molecular weight bands in Western blots?

When NXPH2 antibodies reveal unexpected molecular weight bands in Western blots, a systematic investigation approach is necessary:

• Verification of Expected NXPH2 Molecular Weight:

  • The calculated molecular weight of NXPH2 is approximately 30 kDa

  • Post-translational modifications may cause slight variations in apparent molecular weight

• Analysis of Higher Molecular Weight Bands:

  • Potential protein aggregation: Include reducing agents (DTT or β-mercaptoethanol) in sample buffer

  • Possible dimers or multimers: Try more stringent denaturation conditions

  • Glycosylation or other post-translational modifications: Consider enzymatic treatment (e.g., PNGase F for N-linked glycans)

  • Evaluate cross-reactivity with related neurexophilin family members

• Investigation of Lower Molecular Weight Bands:

  • Potential proteolytic processing: NXPH2 may be processed at the boundary between domains

  • Degradation products: Add additional protease inhibitors during sample preparation

  • Alternative splice variants: Verify against known transcript variants

  • C-terminal or N-terminal fragments: Use antibodies targeting different regions of NXPH2

• Experimental Validation Approaches:

  • Peptide competition assay: Pre-incubate antibody with immunizing peptide to identify specific bands

  • Molecular weight calibration: Use precise molecular weight standards

  • Knockdown/knockout validation: Compare samples with reduced or eliminated NXPH2 expression

  • Immunoprecipitation followed by mass spectrometry to identify protein components

• Technical Optimization:

  • Adjust gel percentage to better resolve proteins in the range of interest

  • Optimize transfer conditions for efficient protein transfer

  • Consider gradient gels for better separation across a wide molecular weight range

• Documentation and Reporting:

  • Clearly document all bands observed and their reproducibility

  • Compare results with published literature on NXPH2

  • Contact antibody manufacturers for technical support and additional validation data

How can inconsistent results between different batches of NXPH2 antibodies be addressed and minimized?

Batch-to-batch variability is a significant challenge, particularly with polyclonal NXPH2 antibodies. These strategies can help address inconsistencies:

• Comprehensive Validation of New Antibody Batches:

  • Perform side-by-side comparison with previous batches

  • Test multiple applications (WB, IHC, IF) to assess performance across platforms

  • Document dilution optimization for each new batch

  • Create a standardized validation protocol specific to your experimental needs

• Reference Sample Archive:

  • Maintain frozen aliquots of standard samples (brain/kidney lysates) for batch testing

  • Use recombinant NXPH2 protein as a consistent positive control

  • Create a reference image library of expected results for comparison

• Quantitative Assessment:

  • Measure signal-to-noise ratios across batches

  • Quantify detection sensitivity using dilution series of positive controls

  • Document epitope-specific reactivity using peptide arrays if available

• Antibody Storage and Handling Optimization:

  • Aliquot antibodies upon receipt to minimize freeze-thaw cycles

  • Follow manufacturer-specific storage recommendations (typically -20°C with 50% glycerol)

  • For frequent use, maintain working aliquots at 4°C (up to one month)

  • Add preservatives (0.02% sodium azide) for long-term storage

• Alternative Strategies:

  • Purchase larger antibody lots when possible to reduce batch changes

  • Consider switching to monoclonal antibodies for greater consistency

  • Validate multiple antibodies targeting different epitopes of NXPH2

  • Implement multiplexed detection approaches combining different NXPH2 antibodies

• Documentation and Quality Control:

  • Maintain detailed records of antibody lot numbers and performance

  • Develop standard operating procedures (SOPs) for antibody validation

  • Consider implementing a rating system for antibody performance across applications

By implementing these practices, researchers can significantly reduce the impact of batch-to-batch variability on experimental outcomes and maintain consistency in NXPH2 detection.

How can computational approaches be leveraged to design and optimize NXPH2-specific antibodies?

Computational approaches are increasingly valuable for designing and optimizing NXPH2-specific antibodies, enabling researchers to move beyond traditional selection methods:

• Epitope Prediction and Selection:

  • Analyze NXPH2 sequence for regions of high antigenicity and surface accessibility

  • Identify conserved regions across species for cross-reactive antibodies

  • Select epitopes distinct from other neurexophilin family members to ensure specificity

  • Target regions less likely to undergo post-translational modifications

• Structure-Based Antibody Design:

  • Utilize protein structure prediction tools to model NXPH2 3D conformation

  • Apply molecular docking simulations to optimize antibody-antigen interactions

  • Identify key binding residues for rational mutation to enhance affinity

  • Implement advanced systems like JAM for de novo antibody design with precise epitope targeting

• Machine Learning Applications:

  • Train models on existing antibody-antigen datasets to predict binding properties

  • Apply deep learning approaches to optimize complementarity-determining regions (CDRs)

  • Use sequence-based predictions to identify frameworks with optimal expression characteristics

  • Implement models that disentangle different binding modes for improved specificity

• Library Design and Screening Optimization:

  • Design natural diversity libraries based on somatic hypermutation patterns

  • Use computational approaches to create focused libraries with higher hit rates

  • Implement in silico screening before experimental validation

  • Apply bacterial display systems to evaluate expression and stability in parallel with binding properties

• Specificity Engineering:

  • Identify key residues that distinguish NXPH2 from other neurexophilin family members

  • Model cross-reactivity potential against similar proteins

  • Design antibodies with customized specificity profiles for either high specificity or controlled cross-reactivity

  • Apply computational tools for negative design against unwanted interactions

• Experimental Validation of Computational Predictions:

  • Implement phage display with high-throughput sequencing for experimental validation

  • Test computationally designed variants with customized specificity profiles

  • Validate predictions through in vitro binding assays and structural studies

  • Iterate between computational predictions and experimental results

These computational approaches not only improve antibody specificity and affinity but can also enhance expression yields and stability, making them valuable tools for developing improved NXPH2 antibodies for research and potential therapeutic applications.

What methodologies can researchers use to study the interaction between NXPH2 and its binding partners, particularly alpha-neurexins?

Studying the interactions between NXPH2 and alpha-neurexins requires sophisticated methodological approaches spanning from biochemical to cellular analyses:

• In Vitro Binding Assays:

  • Surface Plasmon Resonance (SPR): Measure real-time binding kinetics (Kon, Koff) and affinity (KD) between purified NXPH2 and alpha-neurexins

  • Microscale Thermophoresis (MST): Assess binding in solution with minimal protein consumption

  • Bio-Layer Interferometry (BLI): Analyze binding without microfluidics requirements

  • ELISA-Based Interaction Assays: Develop quantitative sandwich assays using NXPH2 antibodies

• Co-Immunoprecipitation Approaches:

  • Use NXPH2 antibodies to pull down protein complexes from neural tissues or cell cultures

  • Perform reciprocal co-immunoprecipitation with alpha-neurexin antibodies

  • Couple with mass spectrometry for unbiased identification of the complete interactome

  • Apply chemical crosslinking to stabilize transient interactions

• Structural Biology Methodologies:

  • X-ray Crystallography: Determine atomic-resolution structures of NXPH2-neurexin complexes

  • Cryo-Electron Microscopy: Visualize larger complexes without crystallization requirements

  • NMR Spectroscopy: Map binding interfaces through chemical shift perturbations

  • Hydrogen-Deuterium Exchange Mass Spectrometry: Identify regions involved in binding

• Cell-Based Interaction Systems:

  • Proximity Ligation Assay (PLA): Visualize interactions in situ with subcellular resolution

  • FRET/BRET Approaches: Measure protein-protein interactions in living cells

  • Split Reporter Systems: GFP complementation or luciferase-based approaches

  • Cell Surface Binding Assays: Using recombinant proteins to identify binding to membrane-expressed partners

• Functional Modulation Experiments:

  • Use NXPH2 antibodies to block interactions with alpha-neurexins

  • Apply gene knockout/knockdown approaches to assess functional consequences

  • Develop peptide mimetics of binding interfaces for competitive inhibition

  • Perform domain swapping or mutagenesis to identify critical binding determinants

• Advanced Imaging Methodologies:

  • Super-Resolution Microscopy: Visualize co-localization at synaptic structures

  • Single-Molecule Tracking: Follow dynamics of NXPH2-neurexin interactions

  • Expansion Microscopy: Achieve enhanced spatial resolution in tissue preparations

  • Correlative Light and Electron Microscopy: Combine functional and ultrastructural data

These complementary approaches provide a comprehensive understanding of NXPH2-alpha-neurexin interactions, from molecular binding mechanisms to functional consequences at synapses.

How can researchers effectively validate the specificity of NXPH2 antibodies across multiple experimental platforms?

Comprehensive validation of NXPH2 antibody specificity across platforms requires a multi-dimensional approach:

• Orthogonal Validation Strategies:

  • Genetic Validation: Test antibodies in tissues/cells with NXPH2 gene knockout or knockdown

  • Peptide Competition: Pre-absorption with immunizing peptide should abolish specific signal

  • Multiple Antibody Concordance: Compare results from antibodies targeting different NXPH2 epitopes

  • Recombinant Protein Controls: Use purified NXPH2 as positive control in multiple assays

• Cross-Platform Technical Validation:

  • Validate in Western blot to confirm molecular weight specificity (expected ~30 kDa)

  • Verify tissue expression pattern in IHC matches known distribution (brain, kidney)

  • Confirm subcellular localization in IF/ICC consistent with secreted protein characteristics

  • Assess specificity in immunoprecipitation followed by mass spectrometry

• Cross-Species Reactivity Assessment:

  • Test antibodies against predicted reactive species (human, mouse, rat commonly)

  • Validate conservation of epitope sequences across species using bioinformatics

  • Compare staining patterns between species for consistency

  • Validate in species where genetic models are available

• Specificity Against Related Proteins:

  • Test for cross-reactivity with other neurexophilin family members (NXPH1, NXPH3, NXPH4)

  • Assess potential cross-reactivity with NXPE family proteins

  • Perform immunoblotting against recombinant related proteins

  • Consider heterologous expression systems overexpressing target or related proteins

• Advanced Validation Technologies:

  • Epitope Mapping: Identify precise binding sites using peptide arrays or hydrogen-deuterium exchange

  • Immunodepletion Studies: Sequential immunoprecipitation to demonstrate antibody specificity

  • Multiple Detection Methods: Validate using different secondary antibody systems

  • Super-Resolution Microscopy: Confirm expected localization patterns with nanoscale precision

• Documentation and Reporting Standards:

  • Document validation across all experimental conditions and platforms

  • Report experimental details including antibody catalog numbers and lot numbers

  • Include all validation controls in publications

  • Consider registering antibodies with the Research Resource Identifiers (RRID) database

This comprehensive validation strategy ensures that experimental results with NXPH2 antibodies are robust, reproducible, and truly reflect the biological properties of NXPH2 rather than technical artifacts.

What approaches can be used to optimize NXPH2 antibody stability and expression for research applications?

Optimizing NXPH2 antibody stability and expression requires consideration of multiple parameters throughout the antibody production and handling processes:

• Framework Optimization for Enhanced Expression:

  • Leverage naturally occurring somatic hypermutation diversity to identify stabilizing frameworks

  • Use bacterial antibody display (BAD) systems to screen variants for improved expression

  • Identify framework residues that influence expression levels through systematic mutation

  • Apply computational approaches to predict stability-enhancing modifications

• Production System Selection and Optimization:

  • Compare expression levels between prokaryotic (E. coli) and eukaryotic systems (mammalian cells, insect cells)

  • Optimize codon usage for the selected expression host

  • Evaluate different signal peptides for improved secretion

  • Test various induction conditions and expression temperatures

• Purification Strategy Optimization:

  • Implement affinity chromatography with protein A/G for IgG formats

  • Consider ion exchange chromatography as a polishing step

  • Use size exclusion chromatography to remove aggregates

  • Optimize buffer conditions during purification to maintain stability

• Formulation for Enhanced Stability:

  • Test different buffer systems (phosphate, Tris, HEPES) at various pH values

  • Add stabilizing excipients (sugars, amino acids, surfactants)

  • Include 50% glycerol for long-term storage at -20°C

  • Add appropriate preservatives (0.02% sodium azide) for extended shelf life

• Storage and Handling Optimization:

  • Aliquot antibodies to minimize freeze-thaw cycles

  • Maintain working stocks at 4°C for up to one month for frequent use

  • Store long-term at -20°C in stabilizing buffer with glycerol

  • Monitor stability through periodic quality control testing

• Stability Enhancement Through Protein Engineering:

  • Identify and remove hydrophobic patches prone to aggregation

  • Engineer disulfide bonds for increased thermostability

  • Remove deamidation-prone asparagine residues

  • Consider humanization approaches for improved stability

• Validation of Optimization Success:

  • Assess thermostability through differential scanning fluorimetry

  • Monitor accelerated stability studies under stress conditions

  • Evaluate long-term activity retention through functional assays

  • Test freeze-thaw stability over multiple cycles

How can researchers design experiments to understand the role of NXPH2 in neurological function using antibody-based approaches?

Designing experiments to investigate NXPH2's role in neurological function using antibody-based approaches requires integrating multiple methodologies:

• Expression Mapping in Neural Systems:

  • Comprehensive Brain Region Analysis: Map NXPH2 expression across brain regions using IHC with validated antibodies

  • Developmental Time Course: Track expression changes during neural development

  • Cell-Type Specificity: Combine with neuronal, glial, and synaptic markers for co-localization studies

  • Subcellular Localization: Use immunogold electron microscopy for precise synaptic localization

• Functional Perturbation Studies:

  • Acute Neutralization: Apply function-blocking NXPH2 antibodies in electrophysiological recordings

  • Chronic Interference: Introduce antibodies to neuronal cultures for long-term functional assessment

  • In Vivo Applications: Use intracerebroventricular antibody delivery for behavioral studies

  • Ex Vivo Preparations: Apply antibodies to brain slices for circuit-level analysis

• Protein-Protein Interaction Analysis:

  • Synaptic Interactome Mapping: Use NXPH2 antibodies for immunoprecipitation coupled with mass spectrometry

  • In Situ Interaction Visualization: Apply proximity ligation assays to visualize NXPH2-neurexin interactions

  • Competition Studies: Use soluble NXPH2 and anti-NXPH2 antibodies to disrupt native interactions

  • Activity-Dependent Dynamics: Analyze how neural activity modulates NXPH2 interactions

• Pathophysiological Relevance Assessment:

  • Disease Model Evaluation: Compare NXPH2 expression and localization in neurological disorder models

  • Human Tissue Studies: Examine NXPH2 patterns in post-mortem samples from patients with neurological conditions

  • Biomarker Potential: Develop sensitive ELISA using NXPH2 antibodies for CSF or serum detection

  • Therapeutic Exploration: Test antibody-based modulation of NXPH2 function in disease models

• Advanced Imaging Approaches:

  • Live Imaging: Use fluorescently-labeled antibody fragments to track NXPH2 dynamics

  • Super-Resolution Microscopy: Resolve NXPH2 distribution at synapses with nanoscale precision

  • Array Tomography: Combine ultrathin sectioning with immunofluorescence for 3D reconstruction

  • Expansion Microscopy: Achieve enhanced spatial resolution in complex neural tissues

• Molecular Mechanism Dissection:

  • Post-Translational Modification Analysis: Use modification-specific antibodies to detect NXPH2 phosphorylation

  • Proteolytic Processing Studies: Develop antibodies specific to different NXPH2 domains to track processing

  • Secretion Pathway Analysis: Track NXPH2 through secretory compartments using compartment markers

  • Receptor Binding and Signaling: Monitor downstream signaling events following NXPH2-neurexin interaction

These experimental approaches provide a comprehensive framework for understanding NXPH2's neurological functions, from molecular mechanisms to circuit-level roles, potentially revealing new insights into synaptic function and neurological disorders.

What are the comparative characteristics of commercially available NXPH2 antibodies?

The following table summarizes key characteristics of commercially available NXPH2 antibodies based on the provided search results:

This comparison allows researchers to select the most appropriate NXPH2 antibody based on their specific experimental requirements, considering factors such as application needs, species reactivity, and available detection systems.

What standardized protocol parameters should be considered for specific NXPH2 antibody applications?

The following table outlines standardized protocol parameters for common NXPH2 antibody applications: