top of page
Streptavidin/Neutravidin ELISA Plates
NIDS® HyperBind Streptavidin/Neutravidin ELISA Plates FAQs
PEG IM ELISA
Wave

FAQs

Quick Search By Topics:

NIDS® HyperBind Streptavidin/Neutravidin ELISA Plates FAQs

PEG immunogenicity ELISA Kit FAQs

What is the intended use of the kit?​

The kit is intended for the detection of anti-Polyethylene Glycol (PEG) antibodies.  A method to detect PEG-specific antibodies in serum and other suitable matrices is necessary to elucidate the immunogenicity of PEGylated biotherapeutics.

Why should I test for anti-PEG antibodies?

PEG polymers have been attached to biotherapeutic drugs to help overcome the inherent immunogenicity of these large molecules.  However, a growing body of published research has shown that PEG itself can be immunogenic.  Please consult the references listed below.​

What type of ELISA method is used by the kit to detect anti-PEG antibodies?

A conventional double antigen bridging ELISA method is used to detect anti-PEG antibodies to the various PEG polymers (related publication).

What is the limit of detection of anti-PEG antibodies with the kit?​

The limit of detection is 125 ng/mL of antibody based on the positive control antibody’s dose-response curve.

What is the length of time necessary to run the kit?​

There is a 2.5 hour turnaround time when using the PEG IM ELISA Kit.

What is the reagent ANPEG-1 provided in the kit?​

ANPEG-1 is the positive control antibody that can be used to run calibrator concentrations and/or quality control samples.  ANPEG-1 is a PEG-specific mouse monoclonal IgM developed at ANP Technologies®, Inc.  ANPEG-1 is capable of binding various linear and branched PEGs with different molecular weights.

Can I report concentrations of ADA from the dose-response curve?​

No.  The dose–response curve you generate with the positive control antibody is used only to demonstrate that the assay is working.  Actual concentrations of ADA should not be calculated from this curve.  ADAs are a diverse population of antibody isotypes and subclasses with a wide range of affinities and avidities.  The positive control antibody cannot represent this diverse population of immune responses.

 

FDA guidelines state that the determination of whether a sample is positive for ADA or not should be based on whether its assay result is above or below a screening cut-point derived from testing actual serum samples from relevant populations.

What is the recommended storage temperature of the kit?​

Store all reagents and kit components at 2-8 oC.  For long term storage, it is recommended that the ANPEG-1 positive control antibody be stored as single-use aliquots at -70 °C.​

What is the kit’s stability?​

Six months at 2-8 °C.​

What is included in the PEG IM ELISA Kit?

The kit includes a PEG Pre-Coated Clear Plate, ANPEG-1, Assay Diluent, PEG Conjugate Reagent, HRP Detector Concentrate, Color Enzyme Reagent, Stop Solution, and plate sealers.

Can the PEG IM ELISA Kit be used to detect antibodies to PEG polymers of varying molecular weights?

Yes. The kit can detect antibodies to PEG of various lengths and with different linking groups.​

Can the components of the PEG IM ELISA kit be purchased individually?​

The positive control antibody ANPEG-1 can be purchased separately along with the Color Enzyme reagent and stop solution.

What is the free drug tolerance of the PEG IM ELISA kit assay?​

A positive result can be detected beyond 100 times excess free PEG.  Complete inhibition occurs at a PEG to antibody ratio of 1000:1 based on drug depletion assays.

What is included in the PEG IM ELISA Kit?

The kit includes a PEG Pre-Coated Clear Plate, ANPEG-1, Assay Diluent, PEG Conjugate Reagent, HRP Detector Concentrate, Color Enzyme Reagent, Stop Solution, and plate sealers.

References

Armstrong JK, Leger R, Wenby RB, Meiselman HJ, Garratty G, Fisher TC. (2003) Occurrence of an antibody to poly(ethylene glycol) in normal donors.  Blood 102:566A

 

Armstrong JK, Hempel G, Koling S, Chan LS, Fisher T, Meiselman HJ, Garratty G. (2007) Antibody against poly(ethylene glycol) adversely affects PEG-asparaginase therapy in lymphoblastic leukemia patients.  Cancer 110:103-111

 

Cheng TL, Chen BM, Chern JW, Wu MF, Roffler SR. (2006)  Efficient clearance of poly(ethylene glycol)-modified immunoenzyme with anti-PEG monoclonal antibody for prodrug cancer therapy.  Bioconj Chem 11:258-266

 

Cheng TL, Cheng CM, Chen BM et al. (2005) Monoclonal antibody-based quantitation of poly(ethylene glycol)-derivatized proteins, liposomes, and nanoparticles.  Bioconj Chem 16:1225-1231

 

Ganson NJ, Kelly SJ, Scarlett E, Sundy JS, Herscfield MS. (2006)  Control of hyperuricemia in subjects with refractory gout, and induction of antibody against poly(ethylene glycol) (PEG), in a phase I trial of subcutaneous PEGylated urate oxidase.  Arthritis Research & Therapy 8:R12

 

Garratty G. (2004) Progress in modulating the RBC membrane to produce transfusable universal/stealth donor RBCs.  Trans Med Rev 18:245-256

 

Leger RM, Arndt P, Garratty G, Armstrong JK, Meiselman HJ, Fisher TC. (2001)  Normal donor sera can contain antibodies to polyethylene glycol (PEG).  Transfusion 41:29S

 

Richter AW, Akerblom E. (1983) Antibodies against polyethylene glycol produced in animals by immunization with monomethoxy polyethylene glycol modified proteins.  Int Arch Allergy Appl Immunol 70:124-131

 

Richter AW, Akerblom E. (1984) Polyethylene glycol reactive antibodies in man: titer distribution in allergic patients treated with monomethoxy polyethylene glycol modified allergens or placebo and in healthy blood donors. Int Arch Allergy Appl Immunol 74:36-39

Protein Extraction Kit FAQs

What compounds comprise endogenous interfering proteins?​

Endogenous interfering proteins can be found in any biological matrix, plasma, serum, whole blood, urine, cerebrospinal fluid, oral fluid, sputum, synovial fluid, etc.  Many bioanalytical methods to detect analytes in these fluids are based on the interaction of a binding pair, such as an antibody and its antigen or a receptor and its ligand.  An interfering protein is any protein that blocks the specific interaction of the binding pair, causing false negative or false positive reactions.​

What kinds of assays are affected by interfering proteins?

Any ligand binding assay such as a sandwich, competitive, or serological immunoassay in ELISA or other format, drug pharmacokinetic (PK) assays, and double antigen bridging immunogenicity (IM) assays are all vulnerable to interfering proteins.

Do I really have to extract or remove these endogenous interfering proteins?​

Some of the interfering proteins, particularly those that do not directly bind analyte, can be blocked in situ by their own specific binding partners, such as antigens, antibodies or binders specific to them.  In such cases, extraction or removal of interfering endogenous proteins is not necessary.

How do endogenous interfering proteins affect IM and PK Assays?​

The double antigen bridging immunoassay is the most useful format for IM assays.  In these assays, an anti-drug antibody (ADA) in the patient sample will form a detectable bridging complex by binding two labeled drug molecules.

 

For therapeutic monoclonal antibodies and similar biotherapeutics that function by binding and blocking disease-associated active proteins, the drug’s target molecule can by itself create a bridging or sandwich complex with the drug conjugate reagents in the IM assay.  This target interference leads to a false positive result in IM assays in the absence of ADA.
 

The endogenous interfering proteins can also bind with a biologic drug in a PK assay, which may significantly alter its PK profile.

Doesn’t acid dissociation take care of this problem in an IM assay?​

Acid dissociation by itself will not resolve this problem.  After neutralization, the interfering protein or drug target will still be around to create a bridging complex that mimics an ADA positive bridging complex in the IM assay, thus still generating false positive results.

Will other approaches like a blocking antibody remove the target interference?​

A separate blocking antibody that will bind interfering target proteins prior to running an immunogenicity assay may work.  Once blocked, the target molecules can no longer form bridging complexes with the drug conjugate reagents.   However, these blocking antibodies can be separated from the interfering target molecules upon acid dissociation, thus removing their corrective effect.  They may then not have enough time to re-block target molecules after the neutralization step before the IM assay is run.  Remember, it is always recommended that the IM assay procedure be run immediately after acid dissociation.

Can’t I then add my blocker at the neutralization step?

If added with the neutralization step or immediately after, the blocker will still not have enough time to bind target proteins since the IM assay has to be run immediately.  A false positive result may still be obtained due to target interference.

What is the best solution to the endogenous protein or drug target interference problem?

The simplest approach is to irreversibly extract or scavenge the interfering endogenous proteins prior to running the IM or PK assay.  The NIDS® NPX4000 Interfering Protein Extraction and Removal Kits enable the irreversible removal of these interfering endogenous proteins without affecting the detection of ADAs in an IM assay or drug molecules in a PK assay.  By attaching your specific blocking antibody or binder to activated nanoparticles and pretreating the sample with these functionalized nanoparticles which will bind the interfering proteins, this simple and easy-to-use protein extraction and removal kit can cleanly sequester such interfering proteins via a centrifugation step.  As a result, more than 99% of the interfering proteins or drug target can be removed, while using significantly less blocking antibody or binder than any other conventional blocking methods.​

What specific endogenous proteins can be removed using these nanoparticles?

We have a list of 140 target proteins which we can extract from test samples using specific antibodies.  ANP can prepare the specific extraction nanoparticle kit for your unique requirements.  Alternatively, you can send us your preferred antibody or binding agent and we can prepare the extraction kit for your use.​

What advantages in terms of capacity and efficiency do your nanoparticles offer?​

Compared to current mainstream methods which use magnetic particles 1 – 5 microns in size, our particles are less than 90 nm in diameter, offering greater surface area and more efficient diffusion through samples resulting in significantly greater extraction capacity and enhanced efficiency of interferant removal.  Consequently, our nanoparticles can remove as much as 1 µg/mL of specific protein.​

Is there anything unique in your coating chemistry that enhances its scavenging efficiency?

Yes.  Our particles use our proprietary Nano-Intelligent Detection System (NIDS®) coating technology which orients the binding sites of the attached agents outwardly for optimal binding.​

What other applications can the nanoparticles be used for? ​

The nanoparticles can be used in protein purification for removal of trace contaminants.​

NIDS® DIY Immunogenicity ELISA Kit FAQs

Why do I need a DIY Immunogenicity ELISA kit?​

The NIDS® Do-it-Yourself (DIY) immunogenicity ELISA Kit enables you to quickly develop a double antigen bridging immunoassay on your own using a straightforward step-by-step method.  This places in your hands a means to significantly accelerate your drug development timetable.​

Does the kit provide me with everything I need?

Yes.  The only things you provide are your biotherapeutic molecule and anti-drug antibody.  Once you receive the kit, you can get started.​

How well does the method work?​

The materials and procedures of the kit have been used in successfully developing immunogenicity assays for multiple biotherapeutics, among which are humanized monoclonal antibodies, humanized chimeric antibodies, receptors, and peptides.

 

Several posters and publications have been recently published describing some of these immunogenicity assays:

1. Pan J, Small T,  Qin D, Li S  ,Wang L, Chen D, Pauley C, Verch T, Kaplanski C, Bakhtiar R, Vallejo YR, Yin R.  Comparison of the NIDS® rapid assay with ELISA methods in immunogenicity testing of two biotherapeutics.   J. Pharm. Tox. Methods63: 150-159 (2011)

 

 

2.  Liu Y, Reidler HA, Pan J, Milunic D, Qin D, Chen D, Vallejo YR, Yin R.  Double Antigen Bridging Immunogenicity ELISA for the Detection of Anti-PEG Antibodies.  American Association of Pharmaceutical Scientists National Biotechnology Conference, San Francisco, CA May 2011 (Abstract)

 

 

3. Pan J, Small T, Qin D., Vallejo Y, Yin R.  NIDS® Rapid Assays for the Detection of Anti-Drug Antibodies to Peptide Drugs.  American Association of Pharmaceutical Scientists National Biotechnology Conference, San Francisco, CA May 2010 (Abstract, received the “Excellence in Ligand Binding Assays” award)

 

 

4. Pan J, Small T., Qin D, Pauley C, Kaplanski C, Verch T, Chen D, Bakhtiar R, Naling Y, Vallejo Y, Yin R.  NIDS® Rapid Assays for the Detection of Anti-Drug Antibodies to Various Polyethylene Glycol (PEG) Polymers.  American Association of Pharmaceutical Scientists National Biotechnology Conference, San Francisco, CA May 2010 (Abstract)

 

If I need assistance, can I obtain it easily?

Yes.  Please call ANP Technologies 302-283-1730 or 302-283-1731 and ask for Technical Support.​

Protein Labeling with Biotin, Digoxigenin, and Fluorescein FAQs

Why do I need to label proteins with biotin, digoxigenin or fluorescein?

When developing ligand binding assays which include immunoassays, DNA/RNA hybridization assays, and other formats, secondary tags are needed to either anchor or capture the complexes that are formed to a solid phase, or to create a means to attach a signal generating moiety such as an enzyme, colored or fluorescent particle or molecule to the complexes formed.

 

These three small molecules are the most commonly used tags. Each one has its own specific binding partner that can be used for capturing compounds or signal-producing molecules tagged with such small molecules.

 

A biotin-labeled molecule can therefore be captured or bound by streptavidin or neutravidin. A digoxigenin- or fluorescein-labeled compound can be captured or bund by antibodies specific to each.

How can I capture a complex formed by a compound tagged with biotin, digoxigenin, or fluorescein?​

Their binding partners can be coated or immobilized onto various surfaces such as plastics, glass, porous membranes, particles, etc. For example, streptavidin can be coated on 96-well plates in order to capture biotinylated proteins or an anti-digoxigenin or anti-fluorescein antibody can be sprayed on a micro- or nanoparticle to capture digoxigenin- or fluorescein-labeled proteins.

Can you show some examples of these designs?​

 

 

 

 

 

 

 

 

 

 

 

 

 

 

What advantages does ANP Technologies’ DIY labeling kit provide me?​

ANP’s DIY (Do-It-Yourself) biotin or digoxigenin labeling kit increases the binding availability of large molecules and reduces assay backgrounds, thus significantly enhancing assay sensitivity and binding kinetics for ligand binding assays. An added feature of these kits is the rapid, easy-to-use QC test strips provided with each kit.​

Why are the rapid QC test strips such a benefit?​

The current methods to determine the success of labeling require destructive testing of high microgram quantities of the product. In addition, these methods are complex and time-consuming to perform. The rapid QC test strips consume a few nanograms of the product and results are obtained typically in less than a minute.​

Do I need to purchase other materials in addition to the DIY kits?​

No. Each kit contains all you will need to conjugate your compound.

Two sandwich assay examples are shown to the above. These examples illustrate how a combination of biotin and digoxigenin tags can be used as a plug & play method for constructing sandwich pharmacokinetics (PK) and immunogenicity assays. For a sandwich PK assay, the solid phase is first coated with streptavidin. For example, precoated HyperBind Streptavidin and Neutravidin 96-well plates are highly recommended for the most efficient solid phase coating. The biotinylated capture and digoxygenin-tagged detector antibodies can then be used to bind the target analyte to form a sandwich immune-complex, followed by the detection with anti-digoxigenin-HRP conjugate.

 

 

The second example is a double antigen bridging immunogenicity assay for the detection of Anti-Drug Antibodies (ADAs). Two drug conjugates are prepared, one tagged with biotin and the other with Digoxigenin. In the presence of an ADA, the two drug conjugates can form a bridge sandwich complex with the ADA, which is captured on a streptavidin plate. The detection is then completed by the addition of an anti-digoxigenin-HRP conjugate.

 

In either example, digoxigenin can be replaced by fluorescein.

PEG Immunogenicity Rapid Assay FAQs

What is the intended use of the assay?​

The assay is intended for the Point of Care (POC) detection of anti-Polyethylene Glycol (PEG) antibodies in patient sera. A method to detect PEG-specific anti-drug antibodies (ADAs) in serum and other physiological matrices is necessary to elucidate the immunogenicity of PEGylated biotherapeutics. It has been designed for potential use as a screen for pre-existing anti-PEG antibodies in targeted patients.​

Why should I test for anti-PEG antibodies?​

PEG polymers have been attached to biotherapeutic drugs to help overcome the inherent immunogenicity of these large molecules.  However, a growing body of published research has shown that PEG itself can be immunogenic.  A patient with anti-PEG antibodies may therefore suffer morbidity when treated with PEGylated drugs.  At the very least, anti-PEG antibodies can block the PEGylated drug and render such costly medication useless.  Please consult the references listed below.

 

Screening of patients for pre-existing anti-PEG antibodies prior to treatment with PEGylated biotherapeutic drugs is now under serious discussion (Garay and Labaune, 2011)

Are PEGylated small molecule drugs or delivery vehicles also potentially immunogenic?​

Yes, especially if the molecular weight of the PEG polymer used exceeds 10 kDa.

What method is used by the NIDS® rapid assay to detect anti-PEG antibodies?

A conventional double antigen bridging method is used to detect anti-PEG antibodies to the various PEG polymers.

Can you describe the technology used in the NIDS® rapid immunogenicity assays?​

Our rapid assays use a lateral flow or immunochromatographic format, which is the basis of home pregnancy tests.  The reagents use our proprietary Nano-Intelligent Detection System (NIDS®) nano-orienting technology to enhance assay sensitivity and specificity.

A general schematic of our rapid immunogenicity tests is shown in the figure below:

Why is a rapid assay important for immunogenicity testing?

The FDA is seriously considering post-market mandatory immunogenicity monitoring for all biosimilars and biobetters.  The NIDS® Rapid Immunogenicity Assays enable non-centralized POC monitoring of patients to be conducted with ease, not just for PEG-specific antibodies, but for any biotherapeutic molecule.

Can rapid assays also be used for pre-clinical and clinical drug safety studies?​

Definitely.  The results obtained using traditional ELISA immunogenicity assays and rapid assays for a growing number of biotherapeutics are very similar.  Dose-response curves similar to ELISAs’ can be generated with rapid assays.  The testing results for sensitivity, specificity, accuracy, precision, and recovery with patient sera are very similar for both assay methods. This is readily seen in published results (Pan et al, 2011).​

Are there any expected differences between ELISA-based methods and rapid assays?​

ELISA-based assays require washing steps which may disrupt complexes formed by low affinity and low avidity antibodies.  Rapid assays do not require dilution and wash steps, and can detect more low affinity and low avidity anti-drug antibodies than other methods.  In some of our own studies comparing ELISAs and rapid assays, the rapid assays have been able to detect ADAs in serum which the ELISAs missed.  These rapid assay positives were confirmed to be true positives using drug depletion assays.  In addition, it often takes more than 4 hours to complete an ELISA test, as compared to only 25-40 min to complete a rapid assay test.

How does the sensitivity of rapid assays compare to ELISA and no-label methods such as Surface Plasmon Resonance (SPR) immunogenicity methods?

Rapid assays attain the same limits of detection as ELISA-based methods.  SPR IM assays are much less sensitive due to the absence of a label.

What is the limit of detection of anti-PEG antibodies with the kit?

The limit of detection is 125 ng/mL of antibody based on the positive control antibody’s dose-response curve using an affinity purified positive control antibody according to th FDA Guidance.

What is the length of time necessary to run the kit?​

There is a < 40 minute time to result using the PEG Rapid IM Assay.​

What is the reagent ANPEG-1 provided in the kit?

ANPEG-1 is the affinity purified positive control antibody that can be used to run calibrator concentrations and/or quality control samples.  ANPEG-1 is a PEG-specific mouse monoclonal IgM developed at ANP Technologies, Inc.  ANPEG-1 is capable of binding various linear and branched PEGs with different molecular weights.​

Can I report concentrations of ADA from the dose-response curve?​

No.  The dose–response curve you generate with the positive control antibody is used only to demonstrate that the assay is working.  Actual concentrations of ADA should not be calculated from this curve.  ADAs are a diverse population of antibody isotypes and subclasses with a wide range of affinities and avidities.  The positive control antibody cannot represent this diverse population of immune responses.

 

FDA guidelines state that the determination of whether a sample is positive for ADA or not should be based on whether its assay result is above or below a screening cut-point derived from testing actual serum samples from relevant populations.

Do I need a reader to run the Rapid Immunogenicity Assays?​

Yes.  An easy to use handheld reader is required to read the assay test strips.  The unit is highly affordable compared to the cost of ELISA reader/washing systems, MSD Electrochemiluminescence readers, and SPR systems.

What is the recommended storage temperature of the kit?

Store all reagents and kit components at 2-8 °C.  For long term storage, it is recommended that the ANPEG-1 positive control antibody be stored as single-use aliquots at -70 °C.​

What is the kit’s stability?

Six months at 2-8 °C.​

What is included in the PEG Rapid IM Assay Kit?

The kit includes Universal Immunogenicity Rapid Assay Test Strips, ANPEG-1 positive control antibody, and PEG Conjugate Reagent.

Can the PEG Rapid IM Assay be used to detect antibodies to PEG polymers of varying molecular weights?

Yes. The kit can detect antibodies to PEG of various lengths and with different functional groups.​

Can the components of the PEG Rapid IM kit be purchased individually?​

Each component can be purchased separately.​

What is the free drug tolerance of the PEG IM ELISA kit assay?

A positive result can be detected beyond 100 times excess free PEG.  Complete inhibition occurs at a PEG to antibody ratio of 1000:1 based on drug depletion assays.

REFERENCES​

Armstrong JK, Leger R, Wenby RB, Meiselman HJ, Garratty G, Fisher TC. (2003)  Occurrence of an antibody to poly(ethylene glycol) in normal donors.  Blood 102:566A

Armstrong JK, Hempel G, Koling S, Chan LS, Fisher T, Meiselman HJ, Garratty G. (2007) Antibody against poly(ethylene glycol) adversely affects PEG-asparaginase therapy in lymphoblastic leukemia patients.  Cancer 110:103-111

 

Cheng TL, Chen BM, Chern JW, Wu MF, Roffler SR. (2006)  Efficient clearance of poly(ethylene glycol)-modified immunoenzyme with anti-PEG monoclonal antibody for prodrug cancer therapy. Bioconj Chem 11:258-266

 

Cheng TL, Cheng CM, Chen BM et al. (2005) Monoclonal antibody-based quantitation of poly(ethylene glycol)-derivatized proteins, liposomes, and nanoparticles.  Bioconj Chem 16:1225-1231

Ganson NJ, Kelly SJ, Scarlett E, Sundy JS, Herscfield MS. (2006)  Control of hyperuricemia in subjects with refractory gout, and induction of antibody against poly(ethylene glycol) (PEG), in a phase I trial of subcutaneous PEGylated urate oxidase.  Arthritis Research & Therapy 8:R12

 

Garay RP and Labaune JP (2011)  JP Immunogenicity of Polyethylene Glycol. The Open Conference Proceedings Journal  2, 104-107
 

Garratty G. (2004) Progress in modulating the RBC membrane to produce transfusable universal/stealth donor RBCs.  Trans Med Rev 18:245-256

 

Leger RM, Arndt P, Garratty G, Armstrong JK, Meiselman HJ, Fisher TC. (2001)  Normal donor sera can contain antibodies to polyethylene glycol (PEG).  Transfusion 41:29S

 

Pan J, Small T,  Qin D, Li S  ,Wang L, Chen D, Pauley C, Verch T, Kaplanski C, Bakhtiar R, Vallejo YR, Yin R. (2011)  Comparison of the NIDS® rapid assay with ELISA methods in immunogenicity testing of two biotherapeutics.   J. Pharm. Tox. Methods 63: 150-159

 

Richter AW, Akerblom E. (1983) Antibodies against polyethylene glycol produced in animals by immunization with monomethoxy polyethylene glycol modified proteins.  Int Arch Allergy Appl Immunol 70:124-131

 

Richter AW, Akerblom E. (1984) Polyethylene glycol reactive antibodies in man: titer distribution in allergic patients treated with monomethoxy polyethylene glycol modified allergens or placebo and in healthy blood donors. Int Arch Allergy Appl Immunol 74:36-39

NIDS® Why should I use NIDS® HyperBind plates?

As a complementNIDS® HyperBind ELISA plates utilize our patented nano-orientation technology that significantly enhances the reactivity of large molecules (> 10 kDa) coated in wells. By optimally orienting these molecules, assay sensitivity may be enhanced by 5 – 100 fold without increasing coating concentrations.

Which NIDS® HyperBind plate should I use, regular-binding or high-binding?

For direct assays such as serological or antibody screening assays with coated antigens, we recommend our NIDS® regular-binding HyperBind Streptavidin and Neutravidin plates. For sandwich ELISAs, we recommend our NIDS® high-binding HyperBind Streptavidin plates.

 

***If the biotinylated compound you wish to coat is in short supply, we recommend using regular-binding HyperBind plates.

Will any biotinylated molecule work with the NIDS® HyperBind plates?

The full advantage of the NIDS® technology can only be achieved when your molecules are biotinylated using the NIDS®DIY biotinylation kits. These labeling kits are easy to use and are unique in providing a rapid and simple Quality Control check to assure you that your molecules have been successfully biotinylated.

Can I coat any concentration of biotinylated protein on your plates?​

The regular-binding plates should be coated at a range of 100 – 2000 ng/mL.  The high binding plates should be coated at 2000 – 5000 ng/mL.  Coating procedures in the Instructions for Use should be strictly followed.​

What is the biotin binding capacity of your plates?

Most Streptavidin and Neutravidin coated plates do not have significant differences in biotin binding capacity, since that property is governed by available surface area in the well and the fact that biotin is a small molecule and will have no issues in orientation and size-related stereochemical blocking and repulsion.   However, our nanomanipulation and nano-orienting chemistry gives us a very high biotinylated protein coating efficiency, allowing more active biotinylated proteins to be coated than conventionally coated plates.​

Can you provide more background information for your plates?​

Please click on the following link:  IVD Technology article​

Protein Extraction
DIY IM ELISA
Protein labelling
PEG IM rarid assay
bottom of page