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SAPS30UM-10
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SHBC
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1%
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30µm
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10ml,20ml,50ml ,500ml,1000ml
30µm Streptavidin Microspheres for Biological Research
SHBC SAPS30UM-10 Streptavidin Microspheres are 30µm surface-functionalized microspheres developed for immobilizing biotinylated antibodies, antigens, proteins, peptides, enzymes, receptors, oligonucleotides, DNA, RNA, aptamers, and other biotin-labeled molecules.
The product is supplied as a 1% solids suspension and is designed for biological assay development, biomolecule immobilization, affinity interaction research, microscopy, cell–particle interaction studies, nucleic acid capture, microfluidics, agglutination research, particle-based biosensors, and research reagent manufacturing.
The 30µm diameter provides a large individual-particle surface and makes the microspheres comparatively easy to observe and manipulate in microscopy and imaging-based systems. The large particle size may also support cell-size-range modeling, individual-particle analysis, size-coded assays, and biological research requiring clearly identifiable microspheres.
Shanghai SanYu Biotechnology Co., Ltd. supports research sample evaluation, pilot-scale development, repeated manufacturing, OEM cooperation, private-label projects, and bulk supply for biotechnology companies, universities, research institutes, reagent developers, instrument manufacturers, and biological research organizations.
Quick Product Answer
SAPS30UM-10 is a 30µm streptavidin-coated microsphere suspension supplied at 1% solids. Its streptavidin-functional surface captures biotinylated biomolecules for antibody and protein immobilization, nucleic acid capture, biological assays, microscopy, cell–particle interaction studies, microfluidics, agglutination research, and particle-based detection-system development.
Product Highlights
Product name: 30µm Streptavidin Microspheres
Catalog number: SAPS30UM-10
Brand: SHBC
Manufacturer: Shanghai SanYu Biotechnology Co., Ltd.
Nominal particle diameter: 30µm
Surface modification: Streptavidin
Solids content: 1%
Binding principle: Streptavidin–biotin affinity
Physical form: Aqueous microsphere suspension
Primary application: Biological research and bead-based assays
Supply capability: Samples, pilot batches, and bulk production
Customization: Available according to technical feasibility
Intended use: Research use only
What Are SAPS30UM-10 Streptavidin Microspheres?
SAPS30UM-10 consists of 30µm microspheres with streptavidin immobilized on the particle surface.
The streptavidin coating provides binding sites for biotinylated molecules. Researchers can attach a selected biotinylated antibody, protein, peptide, nucleic acid probe, aptamer, receptor, lectin, ligand, or other biomolecule without directly activating the microsphere surface with EDC/NHS chemistry.
After a biotinylated capture molecule has been immobilized, the functionalized particles can serve as a solid phase for:
Target capture
Biomolecule immobilization
Antibody screening
Protein interaction analysis
Nucleic acid hybridization
Cell-surface binding research
Microscopy-based detection
Particle-based biosensors
Agglutination studies
Microfluidic research
Imaging-based biological assays
Affinity capture experiments
Potential biotinylated capture molecules include:
Monoclonal antibodies
Polyclonal antibodies
Recombinant antibodies
Antibody fragments
Antigens
Recombinant proteins
Peptides
Enzymes
Receptors
Lectins
Growth factors
Oligonucleotide probes
DNA probes
RNA probes
PCR products
Aptamers
Biotinylated small molecules
Streptavidin-coated microspheres are widely used as a matrix for immobilizing biotinylated antibodies, proteins and nucleic acid probes. The final performance depends on the streptavidin coating, ligand biotinylation, surface accessibility, buffer, mixing and washing conditions.
The 30µm particle diameter provides more physical surface per individual particle than smaller microspheres. However, at the same mass concentration, larger microspheres provide fewer individual particles than smaller microspheres.
SAPS30UM-10 is therefore particularly suitable when the project prioritizes:
Large surface per individual particle
Direct optical observation
Individual-particle analysis
Cell-size-range particle modeling
Size-based particle differentiation
Controlled particle manipulation
Microscopy and imaging
Microfluidic transport
Large-particle agglutination
Easy visual confirmation of particle recovery
SAPS30UM-10 is supplied as a research raw material. It should not automatically be described as a finished diagnostic reagent, certified particle standard, absolute counting bead, magnetic separation bead, or fluorescent coding bead unless those features are specifically included in the final technical specification.
SAPS30UM-10 Technical Specifications
Parameter | Specification |
|---|---|
Product name | 30µm Streptavidin Microspheres |
Catalog number | SAPS30UM-10 |
Brand | SHBC |
Manufacturer | Shanghai SanYu Biotechnology Co., Ltd. |
Nominal particle diameter | 30µm |
Surface modification | Streptavidin coated |
Solids content | 1% |
Physical form | Microsphere suspension |
Binding principle | Streptavidin–biotin affinity |
Compatible ligands | Biotinylated biomolecules |
Primary application | Biological research and bead-based assays |
Supply format | Samples, pilot batches, and bulk quantities |
Intended use | Research use only |
The following values should be confirmed using the final product specification or lot-specific Certificate of Analysis:
Particle matrix
Mean particle diameter
Particle-size range
Particle-size distribution
Particle-size coefficient of variation
Particle morphology
Particle density
Streptavidin coating level
Biotin-binding capacity
Particle number concentration
Suspension buffer
Buffer pH
Stabilizer or surfactant
Preservative
Recommended recovery method
Package size
Shelf life
Storage conditions
Direct competitor pages commonly expose exact diameter, surface functionality, concentration, package size and technical documentation in the product specification area. The same information architecture should be used for SAPS30UM-10 once the corresponding SHBC test data are available.
Biotin-binding capacity should be reported together with:
Type of biotinylated test probe
Probe molecular weight
Biotinylation level
Binding buffer
Incubation time
Incubation temperature
Washing procedure
Detection method
Calculation basis
Lot-specific result
The 1% solids value alone cannot determine particle number concentration or available biotin-binding capacity.
How Streptavidin–Biotin Binding Works
Streptavidin is a biotin-binding protein that enables stable, non-covalent attachment of biotinylated molecules to a microsphere surface.
When a biotinylated ligand is mixed with SAPS30UM-10, the biotin group binds to available streptavidin sites on the particle.
The general structure can be represented as:
Microsphere Surface – Streptavidin – Biotin – Capture Molecule
For an antibody-based sandwich assay, the structure may be:
Microsphere – Streptavidin – Biotinylated Capture Antibody – Target Antigen – Detection Antibody
The detection antibody may carry a fluorescent, enzymatic, colorimetric, chemiluminescent, or other measurable reporter.
Advantages of Streptavidin–Biotin Immobilization
Direct EDC/NHS activation is normally unnecessary for loading a biotinylated ligand.
One microsphere platform can be used with different biotinylated biomolecules.
Antibodies, proteins, peptides and nucleic acid probes can be immobilized.
Ligand loading can be conducted under relatively mild aqueous conditions.
The capture molecule can be changed without redesigning the base particle.
The system supports modular assay development.
Ligand loading can be optimized separately from target detection.
Different reporter systems can be used with the same capture particle.
The platform may support single-target and multiplex research.
Factors Affecting Binding Performance
Final binding and assay performance may be affected by:
Streptavidin coating density
Streptavidin activity
Number of biotin groups per ligand
Location of the biotin groups
Biotin accessibility
Spacer length
Ligand molecular size
Ligand purity
Ligand aggregation
Surface crowding
Buffer composition
Salt concentration
Incubation time
Incubation temperature
Mixing method
Particle settling
Free biotin can occupy available streptavidin sites and reduce capture-ligand loading. Biotinylated molecules should therefore be purified when residual free biotin or excess biotinylation reagent may be present.
Why Choose 30µm Streptavidin Microspheres?
Large Surface per Individual Particle
A 30µm microsphere provides a larger physical surface per individual particle than a 20µm, 10µm, 5µm, or 3µm microsphere.
This may be useful when:
A large amount of capture molecule is required per individual particle
Strong signal generation per particle is desired
Individual particles will be analyzed separately
Surface-binding distribution will be observed by microscopy
A cell-size-range synthetic model is required
Localized binding or surface patterning is being investigated
A larger particle does not necessarily provide greater total surface area per unit mass. Smaller particles normally provide more particles at the same mass concentration.
Excellent Microscopy Visibility
The 30µm diameter makes individual particles comparatively easy to locate using suitable optical microscopy.
Potential imaging methods include:
Bright-field microscopy
Phase-contrast microscopy
Fluorescence microscopy
Confocal microscopy
Imaging flow cytometry
Automated high-content imaging
Microscopy may be used to evaluate:
Particle morphology
Surface fluorescence
Ligand distribution
Aggregation
Cell–particle interactions
Particle recovery
Size-based differentiation
Microfluidic movement
Suitable for Cell-Size-Range Research
The 30µm particle diameter is within the size range of many large cells and cell-like biological structures.
Potential research directions include:
Synthetic cell-model studies
Cell-sized particle transport
Cell–particle contact research
Phagocytosis and uptake studies
Cell-surface receptor binding
Immune-cell interaction research
Microfluidic cell-model testing
Imaging-system development
Synthetic microspheres do not reproduce all optical, mechanical, chemical or biological properties of living cells. Suitability as a cell model must be validated for the intended project.
Clear Particle Identification
The large particle size allows SAPS30UM-10 to be separated visually from many small background particles and debris.
This can be useful in:
Microscopy
Automated imaging
Particle counting
Microfluidic sorting
Agglutination analysis
Size-coded assays
Individual-particle tracking
Practical Recovery and Manipulation
Large particles may be recovered using an optimized centrifugation, filtration, sedimentation or particle-picking method.
The most appropriate method depends on:
Particle material
Particle density
Processing volume
Centrifugal force
Centrifugation time
Filter pore size
Tube geometry
Buffer viscosity
Surfactant concentration
Required particle recovery
Suitable for Size-Coded Multiplex Research
A 30µm population may be combined with smaller microsphere populations in research systems that distinguish particles by size.
Potential applications include:
Multi-analyte assays
Internal process controls
Imaging-based multiplex assays
Microfluidic sorting
Particle-tracking experiments
Multiple capture-ligand populations
Key Features and Benefits
30µm Nominal Particle Diameter
The large particle size supports direct observation, individual-particle analysis, size-based identification and cell-size-range biological research.
Streptavidin-Functional Surface
The surface captures biotinylated antibodies, antigens, proteins, peptides, enzymes, receptors, oligonucleotides, DNA, RNA, aptamers and other biotin-containing molecules.
1% Solids Suspension
SAPS30UM-10 is supplied at 1% solids and can be diluted according to the required particle number, reaction volume, binding capacity and detection method.
Simple Ligand Immobilization
Biotinylated capture molecules can be attached without direct chemical activation of the microsphere surface by the end user.
Large Surface per Particle
Each 30µm microsphere provides a comparatively large physical surface for ligand immobilization and particle-associated signal generation.
Multiple Detection Platforms
The microspheres may be evaluated with:
Optical microscopy
Fluorescence microscopy
Confocal microscopy
Imaging flow cytometry
Conventional flow cytometry where fluidics permit
Microfluidic systems
Plate-based imaging
Particle-counting systems
Colorimetric detection
Fluorescent detection
Agglutination imaging
Modular Biological Assay Platform
The same particle platform can be combined with different biotinylated capture molecules for different research projects.
Bulk Manufacturing Capability
SHBC supports laboratory samples, pilot batches, repeated manufacturing, OEM cooperation and bulk supply.
Custom Development Options
Particle diameter, streptavidin loading, binding capacity, solids content, buffer, preservative, fluorescent coding, visible color, packaging and release specifications may be discussed for qualified projects.
Biological Research Applications
Bead-Based Immunoassay Development
SAPS30UM-10 may be used as the solid phase in sandwich, indirect, competitive or particle-agglutination research assays.
A typical sandwich assay may include:
Immobilization of a biotinylated capture antibody.
Blocking of the remaining particle surface.
Incubation with the test sample.
Capture of the target analyte.
Addition of a labeled detection antibody.
Removal of unbound reagents.
Measurement of particle-associated signal.
Potential research targets include:
Antibodies
Antigens
Cytokines
Hormones
Growth factors
Enzymes
Biomarkers
Pathogen-associated proteins
Food-safety analytes
Environmental targets
Veterinary research targets
Research compounds
Competitive Binding Assays
Competitive assay formats may be evaluated for:
Small molecules
Haptens
Peptides
Drugs
Toxins
Hormones
Metabolites
Targets with limited accessible binding sites
The relationship between target concentration and signal depends on the specific assay design.
Antibody Immobilization and Screening
Biotinylated antibodies may be attached for:
Antigen detection
Antibody screening
Hybridoma screening
Specificity studies
Cross-reactivity evaluation
Affinity comparison
Capture-antibody selection
Assay feasibility testing
Biomarker research
Protein and Peptide Interaction Research
Biotinylated proteins and peptides may be immobilized to investigate:
Antibody–antigen interactions
Protein–protein binding
Receptor–ligand interactions
Epitope recognition
Enzyme–substrate binding
Inhibitor screening
Drug-candidate binding
Protein-affinity comparison
Nucleic Acid Capture and Hybridization
Biotinylated oligonucleotides, DNA, RNA, PCR products and aptamers may be attached to SAPS30UM-10.
Potential applications include:
Sequence-specific capture
Hybridization assay development
PCR-product capture
Genotyping research
Mutation-detection research
Aptamer-based detection
DNA–protein interaction analysis
RNA-binding research
Molecular assay development
Cell–Particle Interaction Research
When coated with an appropriate biotinylated antibody, receptor, lectin, ligand or peptide, SAPS30UM-10 may be evaluated for interaction with cells.
Potential research directions include:
Cell-surface receptor recognition
Cell adhesion
Ligand-mediated cell binding
Immune-cell interaction
Cellular uptake
Phagocytosis
Particle internalization
Cell sorting research
Synthetic antigen-presenting particle research
Important variables include:
Capture-ligand density
Particle-to-cell ratio
Cell concentration
Incubation time
Incubation temperature
Mixing method
Washing conditions
Cell viability
Particle aggregation
Non-specific attachment
Microscopy and High-Content Imaging
The 30µm particles may support:
Bright-field imaging
Phase-contrast imaging
Fluorescence imaging
Confocal microscopy
High-content screening
Particle localization
Cell–particle interaction imaging
Surface-binding analysis
Automated particle classification
Microfluidic Research
SAPS30UM-10 may be evaluated in:
Particle transport studies
Microchannel flow research
Size-based separation
Particle trapping
Hydrodynamic focusing
Imaging in microfluidic devices
Cell-sized particle manipulation
Device-performance testing
The narrowest channel, valve, filter and connector must be compatible with 30µm particles.
Agglutination Research
Large streptavidin microspheres may be evaluated in research methods where target binding or bridging molecules produce measurable particle clustering.
Agglutination may be analyzed through:
Optical microscopy
Automated imaging
Light scattering
Sedimentation patterns
Particle-count changes
Image-analysis algorithms
The relationship between aggregation and analyte concentration must be optimized experimentally.
Particle-Based Biosensors
SAPS30UM-10 may serve as a visible solid-phase carrier in:
Optical biosensors
Imaging-based biosensors
Microfluidic biosensors
Fluorescent particle assays
Enzyme-linked particle assays
Surface-binding studies
Compatible Biotinylated Biomolecules
Biotinylated Antibodies
Potential formats include:
Full-length IgG
IgM
Fab fragments
F(ab′)₂ fragments
Recombinant antibodies
Single-chain variable fragments
Single-domain antibodies
Engineered antibody formats
Antibody activity after immobilization depends on:
Biotinylation chemistry
Number of biotin groups
Location of the biotin groups
Spacer length
Protein purity
Antibody aggregation
Surface loading
Storage conditions
Biotinylated Proteins
Potential examples include:
Recombinant antigens
Enzymes
Cytokines
Growth factors
Receptors
Lectins
Binding proteins
Fusion proteins
Protein standards
Biotinylated Peptides
Potential uses include:
Epitope mapping
Antibody screening
Receptor-binding studies
Enzyme research
Protein interaction studies
Drug-screening assays
A suitable spacer between biotin and the peptide may improve molecular accessibility.
Biotinylated Nucleic Acids
Compatible formats may include:
Single-stranded DNA
Double-stranded DNA
RNA
Oligonucleotide probes
PCR amplicons
Aptamers
Modified nucleic acid probes
Capture sequences
Biotinylated Small Molecules
Small biotinylated compounds may be immobilized when their biotin groups remain accessible to the streptavidin surface.
Spacer design and molecular orientation should be considered during method development.
Recommended Biotinylated Ligand Loading Protocol
The following procedure is a general development starting point. Final conditions should be optimized for the actual biomolecule and application.
1. Resuspend SAPS30UM-10
Allow the suspension to reach the recommended handling temperature.
Mix by gentle inversion, rotation or controlled vortexing until the suspension is homogeneous.
Because 30µm particles can settle quickly, mix the stock immediately before every sampling step.
During repeated dispensing, maintain gentle mixing or remix the suspension before each aliquot.
2. Calculate the Required Particle Amount
Determine the required quantity according to:
Number of tests
Number of particles required per test
Surface required per reaction
Reaction volume
Expected target concentration
Lot-specific binding capacity
Number of wash steps
Expected processing loss
Do not estimate ligand-loading capacity from the solids concentration alone.
3. Transfer the Microspheres
Transfer the required volume to a clean, low-binding tube or processing vessel.
Use a pipette tip with an opening suitable for 30µm particles.
Avoid narrow tips that may restrict particle transfer or produce inconsistent particle numbers.
4. Wash the Microspheres
Wash the particles using a binding buffer compatible with streptavidin and the selected biotinylated ligand.
Avoid free biotin during ligand immobilization.
Potential recovery methods include:
Centrifugation
Membrane filtration
Controlled sedimentation
Cell-strainer-based recovery
Other validated solid–liquid separation methods
The method should be established using the actual particle material, density, buffer, processing volume and required recovery.
5. Prepare the Biotinylated Ligand
Dilute the selected biomolecule in a compatible binding buffer.
Review:
Ligand concentration
Biotinylation level
Molecular purity
Aggregate level
Free biotin content
Residual biotinylation reagent
Buffer additives
Protein stability
Nucleic acid stability
6. Add the Ligand
Combine the washed particles with the biotinylated ligand.
Use gentle rotation, rocking or controlled mixing to keep the microspheres suspended.
Avoid excessive vortexing, foaming and mechanical conditions that may damage the biomolecule.
7. Optimize the Incubation
Evaluate:
Microsphere concentration
Ligand concentration
Ligand-to-particle ratio
Incubation time
Incubation temperature
Buffer pH
Salt concentration
Mixing speed
Reaction volume
Continuous gentle mixing is especially important for 30µm particles because sedimentation may produce uneven ligand exposure.
8. Remove Unbound Ligand
Separate and wash the particles to remove unbound biotinylated molecules.
Insufficient washing may increase background, while excessive washing may reduce particle recovery.
9. Block the Particle Surface
Incubate the ligand-loaded microspheres with an application-compatible blocking reagent.
Potential blocking materials include:
Bovine serum albumin
Casein
Fish gelatin
Non-immune immunoglobulin
Synthetic blocking polymers
Commercial particle-blocking buffers
The blocker should reduce negative-sample signal without substantially reducing target-specific binding.
10. Resuspend the Prepared Microspheres
Resuspend the coated and blocked particles in a suitable assay or storage buffer.
Evaluate:
Particle dispersion
Ligand retention
Binding activity
Non-specific binding
Particle recovery
Settling behavior
Redispersion
Short-term stability
Long-term stability
Microbial stability
Recommended Biological Assay Workflow
1. Prepare Capture Microspheres
Load SAPS30UM-10 with the selected biotinylated capture molecule.
Wash and block the particles before sample testing.
2. Prepare Controls
Recommended controls may include:
Assay-buffer blank
Streptavidin microspheres without capture ligand
Capture-ligand-loaded microspheres without target
Negative sample
Positive sample
Reporter-only control
Isotype control
Non-relevant biotinylated ligand control
Unlabeled target control
Single-color controls when fluorescence is used
3. Add the Test Sample
Combine the prepared microspheres with the test sample.
Optimize:
Sample volume
Sample dilution
Particle concentration
Particles per reaction
Target concentration range
Incubation time
Incubation temperature
Mixing method
Sample matrix
Maintain gentle mixing throughout the incubation.
4. Wash the Particles
Remove unbound sample components while maintaining acceptable recovery.
Record:
Number of washes
Wash-buffer composition
Wash volume
Separation method
Residual supernatant volume
Mixing procedure
5. Add the Detection Reagent
Add a fluorescent, enzymatic, colorimetric, chemiluminescent or other compatible reporter.
The selected detection system must match the intended assay platform.
6. Incubate and Wash
Optimize reporter concentration and incubation time.
Remove unbound detection reagent to reduce background.
7. Resuspend for Detection
Resuspend the particles in a clean detection buffer.
Mix immediately before transferring the sample to the instrument, slide, microplate or imaging chamber.
8. Measure the Signal
Potential analytical outputs include:
Mean particle fluorescence
Median particle fluorescence
Percentage of positive particles
Surface fluorescence distribution
Signal-to-background ratio
Particle-associated enzyme activity
Color intensity
Agglutination level
Particle-count changes
Dose-response curve
Assay precision
Recovery
Specificity
Cross-reactivity
9. Analyze the Results
Establish positive and negative thresholds using appropriate controls.
Do not define a positive result using the test sample alone.
Handling, Mixing and Sampling of 30µm Microspheres
Rapid Settling
The 30µm microspheres may settle more rapidly than smaller particles.
Settling can cause:
Unequal particle concentrations
Variation between aliquots
Inconsistent ligand loading
Different particle counts between reactions
Uneven exposure to the sample
Variable assay signals
Reduced reproducibility
Maintaining a Uniform Suspension
Suitable mixing methods may include:
Gentle inversion
End-over-end rotation
Slow orbital mixing
Gentle rocking
Controlled vortexing before sampling
Intermittent pipette mixing
Avoid vigorous mixing that produces foam or damages protein reagents.
Consistent Pipetting
During repeated dispensing:
Mix the stock thoroughly.
Aspirate the required volume promptly.
Dispense the entire volume.
Remix before the next aliquot.
Use the same pipetting technique for all samples.
For large batches, a validated slow-mixing system can help maintain a consistent particle concentration during filling.
Pipette-Tip Selection
Use tips with an opening large enough for unrestricted particle movement.
Very narrow tips may:
Retain particles
Produce uneven particle numbers
Promote aggregation
Reduce delivery accuracy
Increase variation between samples
Particle Recovery and Washing Methods
Centrifugation
Centrifugation may be used when the particle density and suspension formulation permit efficient recovery.
The minimum effective centrifugal force and time should be determined experimentally.
An ideal condition should provide:
Acceptable particle recovery
A manageable particle pellet
Easy redispersion
Minimal aggregation
Limited biomolecule damage
Filtration
A membrane, mesh or cell strainer with a suitable pore size may be used for washing or recovery.
Confirm:
Particle retention
Low non-specific biomolecule adsorption
Acceptable particle recovery
Easy release from the membrane
Compatibility with the processing volume
Controlled Sedimentation
Natural or accelerated sedimentation may be suitable for selected workflows.
Sedimentation-based recovery may reduce mechanical stress but can require longer processing times and careful control of supernatant removal.
Manual Particle Selection
In microscopy or single-particle projects, individual microspheres may be manipulated using:
Micropipettes
Microcapillaries
Micromanipulation systems
Optical or mechanical particle-picking devices
Magnetic Separation
SAPS30UM-10 should not be assumed to be magnetic.
Magnetic separation is only appropriate when the product specification explicitly states that the particles contain a magnetic component.
Microscopy, Flow Cytometry and Microfluidic Detection
Optical Microscopy
The 30µm particles can generally be observed using standard optical microscopy.
Potential uses include:
Morphology evaluation
Aggregate inspection
Particle counting
Surface-binding visualization
Cell–particle interaction analysis
Recovery assessment
Size-distribution observation
Fluorescence Microscopy
When the particle carries a fluorescent reporter, internal dye or fluorescently labeled target, fluorescence microscopy may be used to evaluate:
Surface signal
Binding uniformity
Positive and negative particles
Cell–particle interactions
Multiplex populations
Reporter localization
Confocal Microscopy
Confocal imaging may help distinguish surface-associated fluorescence from fluorescence in the surrounding solution and may support three-dimensional analysis of particle-associated binding.
Flow Cytometry
SAPS30UM-10 may be evaluated by flow cytometry only when the instrument fluidics are compatible with 30µm particles.
Before testing, confirm:
Sample tubing diameter
Flow-cell dimensions
Nozzle or orifice size
Narrowest fluidic pathway
Particle concentration
Aggregate level
Sample flow rate
Detector range
Some conventional flow cytometers may not be suitable for particles of this size. Instrument compatibility should be confirmed before routine use.
Imaging Flow Cytometry
The large particle size may be well suited to compatible imaging flow cytometry platforms that combine morphological images with fluorescence measurement.
Microfluidic Systems
Before using SAPS30UM-10 in a microfluidic device, confirm that:
Channels are sufficiently wide
Constrictions can pass the particles
Valves and connectors are compatible
Filters will not retain the particles unintentionally
The selected flow rate does not promote blockage
Aggregation is adequately controlled
Blocking and Non-Specific Binding Control
Non-specific adsorption may increase background and reduce assay sensitivity.
Potential causes include:
Inadequate blocking
Incompatible blocking reagent
Excess capture ligand
Excess detection reagent
Insufficient washing
Aggregated antibodies
Hydrophobic sample components
High sample protein concentration
Particle aggregation
Sample-matrix interference
Screen Multiple Blocking Reagents
Compare several blocking formulations.
The preferred blocker should reduce the negative-sample signal while maintaining target-specific binding.
Optimize Capture-Ligand Loading
Maximum ligand loading does not always produce maximum assay performance.
Excessive loading may:
Cause steric crowding
Reduce target accessibility
Increase reagent consumption
Increase non-specific interactions
Increase assay variation
Titrate the Detection Reagent
Excess detection reagent may increase background.
Test several reporter concentrations using positive and negative controls.
Optimize Washing
Evaluate:
Number of wash steps
Wash-buffer composition
Wash volume
Separation method
Mixing method
Residual supernatant
Particle recovery
Evaluate Detergents Carefully
A small amount of compatible detergent may improve particle dispersion and reduce non-specific adsorption.
Excessive detergent may interfere with biomolecule interactions or detection reagents.
Comparison of 30µm, 20µm and 10µm Microspheres
Comparison | SAPS30UM-10 | SAPS20UM-10 | SAPS10UM-10 |
|---|---|---|---|
Nominal diameter | 30µm | 20µm | 10µm |
Solids content | 1% | 1% | 1% |
Surface per individual particle | Largest | Large | Smaller |
Particle number per unit mass | Lowest | Intermediate | Highest |
Settling tendency | Generally highest | High | Lower |
Microscopy visibility | Excellent | Excellent | Very good |
Cell-size-range modeling | Strong relevance | Strong relevance | Relevant |
Fluidic compatibility | Requires careful checking | Requires checking | Generally easier |
Size-coded identification | Very clear | Clear | Clear |
Need for continuous mixing | Highest | High | Moderate |
Individual-particle analysis | Highly suitable | Suitable | Suitable |
Choose SAPS30UM-10 When:
Maximum surface per individual microsphere is preferred.
Direct microscopy is a primary detection method.
A large cell-size-range particle model is required.
Individual-particle analysis is important.
Clear size-based identification is needed.
Microfluidic manipulation is being studied.
Large-particle agglutination research is planned.
Strong visual confirmation of recovery is useful.
Choose SAPS20UM-10 When:
A large microsphere is required with somewhat easier fluidic compatibility.
Microscopy and cell-size-range research are important.
Lower settling than 30µm particles is preferred.
A greater particle number per unit mass is required.
Choose SAPS10UM-10 When:
Conventional flow cytometry is a primary detection method.
More particles per unit mass are required.
Lower settling is preferred.
Smaller reaction volumes will be used.
Easier fluidic compatibility is important.
The final particle size should be selected according to the biological application, detection platform, required particle number, ligand loading, settling behavior, recovery method and instrument compatibility.
Quality Control and Batch Consistency
Potential quality-control parameters for SAPS30UM-10 include:
Mean particle diameter
Particle-size range
Particle-size distribution
Particle-size coefficient of variation
Particle morphology
Suspension appearance
Solids content
Streptavidin coating consistency
Biotin-binding capacity
Particle dispersion
Aggregate level
Settling rate
Redispersion performance
Particle recovery
Background signal
Non-specific binding
Microbial control
Packaging integrity
Storage stability
Lot-to-lot consistency
Particle-Size Testing
Particle-size characterization may include:
Mean diameter
Median diameter
Minimum and maximum size
Size distribution
Coefficient of variation
Microscopy results
Instrumental particle-size analysis
The measurement method should be stated when reporting particle-size data.
Biotin-Binding Capacity
Binding capacity should be measured using a defined biotinylated probe.
The result may be affected by:
Probe type
Molecular size
Biotinylation level
Probe purity
Incubation conditions
Buffer composition
Washing procedure
Detection method
Calculation basis
Binding values obtained with different probes or test methods may not be directly comparable. Bangs Laboratories similarly reports lot-specific binding capacity through the Certificate of Analysis rather than relying only on nominal particle properties.
Functional Quality Control
A functional QC assay may evaluate:
Binding of a standardized biotinylated probe
Percentage of positive particles
Signal distribution
Background separation
Particle recovery
Aggregate percentage
Repeatability
Redispersion after storage
Sampling Consistency
Because 30µm particles settle relatively quickly, filling and sampling procedures should be validated.
Potential controls include:
Continuous gentle mixing during filling
Particle-count testing at the beginning, middle and end of filling
Solids-content verification
Visual homogeneity inspection
Particle-count comparison between containers
Lot-Specific Documentation
Available documentation may include:
Certificate of Analysis
Product specification
Particle-size results
Solids-content results
Binding-capacity results
Safety Data Sheet
Handling instructions
Storage recommendations
Lot number
Production date
Required release tests and acceptance criteria should be agreed upon before bulk manufacturing.
Bulk Manufacturing and Customization
Shanghai SanYu Biotechnology Co., Ltd. supplies SHBC streptavidin microspheres for laboratory research, pilot development, repeated production and enterprise bulk purchasing.
Research Sample Evaluation
Samples may be evaluated for:
Particle morphology
Particle-size distribution
Particle dispersion
Streptavidin activity
Biotinylated ligand loading
Non-specific binding
Particle recovery
Assay feasibility
Microscopy compatibility
Microfluidic compatibility
Settling and redispersion
Pilot-Scale Development
Pilot batches may support:
Assay optimization
Binding-capacity verification
Stability studies
Buffer selection
Preservative evaluation
Packaging evaluation
Filling-process development
Quality-control development
Customer verification
Process transfer
Bulk Production
Bulk manufacturing can be arranged after technical requirements and release specifications have been confirmed.
Please provide:
Required quantity
Expected annual demand
Preferred package size
Intended biological application
Required particle diameter
Required solids content
Required binding capacity
Biotinylated ligand type
Buffer requirements
Preservative restrictions
Quality-control requirements
Documentation requirements
Delivery schedule
Delivery destination
Custom Particle Diameter
Alternative particle sizes may be discussed according to application and manufacturing feasibility.
Custom Streptavidin Loading
Project-specific streptavidin coating levels or binding-capacity targets may be evaluated.
Custom Fluorescence or Color Coding
For imaging and multiplex research, fluorescently encoded or visibly colored streptavidin microspheres may be discussed.
Potential options may include:
Alternative excitation wavelengths
Alternative emission wavelengths
Different fluorescence colors
Multiple fluorescence intensities
Visible particle colors
Customer-specific coding systems
Custom Buffer and Concentration
Alternative solids concentrations, buffer formulations, surfactants, preservative systems and packaging formats may be evaluated.
OEM and Private-Label Supply
Available cooperation formats may include:
OEM packaging
Customer-specific labels
Private-label supply
Customer-specific catalog numbers
Bulk raw material supply
Customized technical documents
Customer-specific release specifications
Storage and Stability Recommendations
Follow the final product label, technical data sheet and lot-specific Certificate of Analysis.
General recommendations include:
Store under the specified refrigerated conditions.
Do not freeze unless freeze–thaw stability has been validated.
Keep the container tightly closed.
Store the vial upright.
Mix thoroughly before sampling.
Maintain the particles in suspension during processing.
Use clean pipette tips and low-binding tubes.
Avoid contamination of the original suspension.
Do not allow the particles to dry.
Avoid repeated unnecessary temperature changes.
Do not return diluted material to the original container.
Record the product lot number and opening date.
Technical guidance from established streptavidin-particle suppliers similarly recommends maintaining the particles in liquid, preventing drying and avoiding freezing.
Settling and Resuspension
Because SAPS30UM-10 contains large particles, settling may occur rapidly.
Before use:
Allow the vial to reach the recommended handling temperature.
Gently invert or rotate the vial.
Apply controlled vortexing when necessary.
Confirm that the suspension is homogeneous.
Mix immediately before sampling.
Continue gentle mixing during repeated dispensing.
Inspect for irreversible aggregates.
Reversible settling does not necessarily indicate product failure.
Avoid Drying
Do not allow the particle pellet to dry during washing.
Drying may cause:
Irreversible aggregation
Reduced streptavidin activity
Difficult redispersion
Increased background
Reduced particle recovery
Avoid Freezing
Freezing may cause:
Particle aggregation
Changes in suspension stability
Reduced protein activity
Reduced particle recovery
Increased assay variability
Evaluate Prepared Reagent Stability
Biotinylated-ligand-loaded and blocked microspheres may have different stability from the original SAPS30UM-10 product.
Evaluate the final prepared reagent under the intended storage, transport and operating conditions.
Troubleshooting Guide
Weak Biotinylated Ligand Binding
Possible causes:
Free biotin in the buffer
Residual biotinylation reagent
Low ligand biotinylation
Inaccessible biotin groups
Insufficient ligand concentration
Inadequate incubation time
Inactive streptavidin
Incompatible buffer
Particle settling during incubation
Recommended actions:
Remove free biotin.
Purify the biotinylated ligand.
Verify the biotinylation level.
Evaluate a suitable spacer.
Maintain continuous gentle mixing.
Increase ligand concentration gradually.
Test a positive-control biotinylated ligand.
High Background Signal
Possible causes:
Insufficient blocking
Excess detection reagent
Inadequate washing
Non-specific reporter adsorption
Sample-matrix interference
Aggregated antibodies
Excess capture-ligand loading
Recommended actions:
Compare different blockers.
Titrate the detection reagent.
Optimize washing.
Remove protein aggregates when appropriate.
Dilute the sample.
Reduce capture-ligand loading.
Unequal Particle Numbers Between Aliquots
Possible causes:
Rapid particle settling
Inadequate stock mixing
Delay between mixing and sampling
Narrow pipette-tip opening
Inconsistent transfer technique
Recommended actions:
Mix before every aliquot.
Use an appropriate pipette tip.
Maintain slow mixing during repeated dispensing.
Standardize the sampling interval.
Verify particle numbers during filling.
Particle Aggregation
Possible causes:
Incompatible buffer
Extreme pH
High ionic strength
Freezing
Drying
Excessive ligand loading
Insufficient stabilizer
Microbial contamination
Recommended actions:
Evaluate buffer compatibility.
Avoid freezing and drying.
Optimize ligand loading.
Use controlled gentle mixing.
Review stabilizer and preservative requirements.
Low Particle Recovery
Possible causes:
Loss during supernatant removal
Adhesion to tubes
Incorrect filter pore size
Incomplete sedimentation
Incomplete transfer
Excessive washing
Particle retention inside pipette tips
Recommended actions:
Use low-binding tubes.
Optimize separation conditions.
Validate the filter or mesh.
Mix before every transfer.
Reduce unnecessary wash steps.
Leave a controlled residual volume above the pellet.
Microfluidic Blockage
Possible causes:
Channel dimensions too small
Particle aggregation
High particle concentration
Narrow connectors
Incompatible valves or filters
Insufficient device flushing
Recommended actions:
Confirm the minimum channel dimension.
Reduce particle concentration.
Remove aggregates before loading.
Increase flow-path dimensions.
Validate the complete device with plain 30µm particles first.
Frequently Asked Questions
What is SAPS30UM-10?
SAPS30UM-10 is a 30µm streptavidin-coated microsphere suspension supplied at 1% solids for capturing biotinylated biomolecules in biological research and particle-based assays.
What is the SHBC brand?
SHBC is the microsphere and biotechnology material brand of Shanghai SanYu Biotechnology Co., Ltd.
What is the nominal particle diameter?
The nominal particle diameter is 30µm.
The measured diameter, size range and particle-size distribution should be confirmed using lot-specific documentation.
What is the solids content?
SAPS30UM-10 is supplied at 1% solids.
Are SAPS30UM-10 microspheres magnetic?
The product should not be assumed to be magnetic unless magnetic properties are specifically stated in the technical specification.
For magnetic separation, select a product specifically described as streptavidin magnetic beads.
Are the microspheres fluorescent?
The standard product should not be assumed to contain an internal fluorescent dye unless fluorescence is specifically stated.
A fluorescently encoded version may be discussed as a custom product.
Which molecules can bind to SAPS30UM-10?
The streptavidin surface can capture biotinylated antibodies, antigens, proteins, peptides, enzymes, receptors, oligonucleotides, DNA, RNA, aptamers and other biotin-containing molecules.
Can an unmodified antibody bind directly?
An unmodified antibody will not specifically attach through the streptavidin–biotin interaction unless it is biotinylated or connected through another compatible reagent.
Is EDC/NHS activation required?
EDC/NHS activation is normally not required when loading a biotinylated molecule onto streptavidin-coated microspheres.
What is the biotin-binding capacity?
Binding capacity should be confirmed using the product specification or lot-specific Certificate of Analysis.
It should not be estimated from solids content alone.
Why choose 30µm microspheres?
The 30µm particles provide a large surface per individual particle, excellent microscopy visibility, clear size-based identification and dimensions suitable for selected cell-size-range research.
Do 30µm particles provide more total surface area?
Each 30µm particle has more surface area than each smaller particle.
However, smaller particles normally provide more particles and greater collective surface area per unit mass.
Why do the particles settle quickly?
Large particles generally settle more quickly than smaller microspheres.
Mix the stock immediately before sampling and maintain gentle mixing during incubation.
Can SAPS30UM-10 be used for microscopy?
Yes. The particle size is suitable for evaluation by optical, fluorescence and confocal microscopy.
Can SAPS30UM-10 be used in flow cytometry?
It may be used only when the flow cytometer fluidics, nozzle, flow cell and sample pathway are compatible with 30µm particles.
Can SAPS30UM-10 be used as a cell model?
The 30µm diameter may be useful in cell-size-range particle research.
Synthetic microspheres do not reproduce all optical, mechanical, chemical or biological properties of living cells.
Can the microspheres be used for immunoassays?
Yes. A biotinylated capture antibody may be immobilized on the particle, followed by target capture and detection with a compatible reporter.
Can the particles be used for nucleic acid capture?
Yes. Biotinylated oligonucleotides, DNA, RNA, PCR products and aptamers may be evaluated for immobilization and target capture.
Can SAPS30UM-10 be used in multiplex assays?
Yes, provided that the 30µm population can be distinguished from other microsphere populations.
Size coding, fluorescence coding or visible color coding may be considered.
How should the particles be washed?
The washing method depends on particle material, density, buffer, volume and required recovery.
Centrifugation, filtration, mesh-based recovery or controlled sedimentation may be evaluated.
How can non-specific binding be reduced?
Optimize the blocking reagent, capture-ligand concentration, detection-reagent concentration, washing conditions, detergent level, sample dilution and incubation time.
Can buffers containing free biotin be used?
Free biotin may occupy streptavidin-binding sites and should generally be avoided during capture-ligand loading.
Should SAPS30UM-10 be diluted before use?
Yes. Prepare a working concentration according to the required particle number, reaction volume and detection method.
Can SAPS30UM-10 be frozen?
Freezing is generally not recommended unless freeze–thaw stability has been specifically validated.
Can the concentration be customized?
Alternative solids concentrations may be discussed according to project requirements and manufacturing feasibility.
Can the binding capacity be customized?
Project-specific streptavidin coating levels or binding-capacity targets may be evaluated.
Can fluorescent 30µm streptavidin microspheres be produced?
Fluorescently encoded or visibly colored 30µm streptavidin microspheres may be discussed for qualified imaging, microfluidic and multiplex projects.
Is bulk production available?
Yes. Shanghai SanYu Biotechnology Co., Ltd. supports samples, pilot batches, repeated orders, OEM projects and bulk manufacturing.
What information is required for a quotation?
Please provide:
Catalog number SAPS30UM-10
Required quantity
Expected annual purchasing volume
Preferred package size
Intended biological application
Type of biotinylated ligand
Required binding capacity
Required particles per test
Detection method
Buffer restrictions
Preservative restrictions
Quality-control requirements
Documentation requirements
Delivery destination
Request a Sample or Bulk Quotation
SHBC SAPS30UM-10 30µm Streptavidin Microspheres provide a large, clearly identifiable particle platform for immobilizing biotinylated antibodies, proteins, peptides, enzymes, receptors, oligonucleotides, DNA, RNA, aptamers and other biotin-labeled molecules.
The product is suitable for:
Biological assay development
Bead-based immunoassays
Antibody immobilization
Protein interaction research
Nucleic acid capture
Hybridization assays
Cell–particle interaction research
Microscopy and imaging
Microfluidic research
Agglutination research
Size-coded multiplex systems
Particle-based biosensors
Research reagent manufacturing
SAPS30UM-10 provides:
30µm nominal particle diameter
Streptavidin-functional surface
1% solids suspension
Large surface per individual particle
Excellent microscopic visibility
Compatibility with biotinylated biomolecules
Sample and pilot-batch supply
Bulk manufacturing capability
OEM and custom-development support
For sample evaluation or bulk purchasing, provide the intended application, required quantity, biotinylated ligand, desired binding capacity, detection platform, packaging requirements and quality-control specifications.
Product Name: 30µm Streptavidin Microspheres
Catalog Number: SAPS30UM-10
Brand: SHBC
Manufacturer: Shanghai SanYu Biotechnology Co., Ltd.
Nominal Particle Diameter: 30µm
Surface Modification: Streptavidin
Solids Content: 1%
Primary Application: Biological Research and Bead-Based Assays
Supply Capability: Samples, Pilot Batches and Bulk Production
Intended Use: Research Use Only. Not for diagnostic or therapeutic use.


