Pierce™ Nickel Coated Plates
Pierce™ Nickel Coated Plates
Pierce™ Nickel Coated Plates
Pierce™ Nickel Coated Plates
Thermo Scientific™

Pierce™ Nickel Coated Plates

Thermo Scientific™ Pierce Nickel Coated Plates provide a simple format to bind His-tagged fusion proteins for ELISA and other plate-based assays involving protein interactions of expressed recombinant proteins.
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Catalog NumberColorFormatDetection Method
15142ClearStrip PlateColorimetric
15342BlackStandardFluorescence
15442ClearStandardColorimetric
15242WhiteStandardChemiluminescence
Catalog number 15142
Price (USD)
-
Color:
Clear
Format:
Strip Plate
Detection Method:
Colorimetric
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These Ni(2+) chelate-coated plates are ideal for analyzing polyhistidine-tagged fusion proteins by ELISA-based methods. Proteins that contain a succession of several histidine residues at the amino or carboxyl terminus have a strong binding affinity for metal. Bacterial lysates containing polyhistidine-tagged fusion proteins can be added directly to the plates without the need for blocking. The clear, white or black plates can be used with colorimetric, chemiluminescent or fluorescent detection methods, respectively.
Thermo Scientific Pierce Nickel Coated White 96-Well Plates provide a simple format to bind His-tagged fusion proteins for ELISA and other plate-based assays involving protein interactions of expressed recombinant proteins. These white plates can be used with chemiluminescent detection methods.

Features of Pierce Nickel Coated Plates include:
• Ni2+ activated surface enables metal-chelate binding of His-tagged proteins
• Detergents used to lyse cells don't inhibit binding to activated plates as they do with plain polystyrene
• Better binding for sensitive assays compared to other commercially available nickel-activated plates
• Detection limit: 1 ng of polyhistidine fusion protein
• Binding capacity: approx. 9 pmol His-tagged protein (27 kDa) per well
• Activation level: 200 μL

These Ni(2+) chelate-coated plates are ideal for analyzing polyhistidine-tagged fusion proteins by ELISA-based methods. Proteins that contain a succession of several histidine residues at the amino or carboxyl terminus have a strong binding affinity for metal. Bacterial lysates containing polyhistidine-tagged fusion proteins can be added directly to the plates without the need for blocking.

For Research Use Only. Not for use in diagnostic procedures.
Specifications
Binding PropertyStandard Capacity, Affinity
Detection MethodColorimetric
Packaging5 Plates
Plate BlockingBlocker™ BSA Buffer
Product TypeMicroplate
Quantity5 plates
ColorClear
FormatStrip Plate
MaterialPolystyrene
No. of Wells96
Product LinePierce
Surface TreatmentDivalent Nickel, Metal Chelate
Volume (Metric) Well200 μL
Unit SizeEach
Contents & Storage
Upon receipt store plates at 4°C in unopened pouches. Once opened, place unused plates in a resealable bag with desiccant and store at 4°C.
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Lot #Certificate TypeDateCatalog Number(s)
3212457Certificate of AnalysisJun 24, 202515342
3212164Certificate of AnalysisJun 21, 202515142
3212459Certificate of AnalysisMay 19, 202515442
AB409089Certificate of AnalysisMar 18, 202515342
AB401373Certificate of AnalysisMar 18, 202515242
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Safety Data Sheets

Frequently asked questions (FAQs)

The water used for washing of microplates as well as all assay reagents, must be of absolutely ultra-pure quality. This means that no metal ions should be present in the water, as this will bind to the His-tag and thereby decrease the binding of the fusion protein to the nickel-chelate complex.

Yes. For instance, use imidazole in concentrations >500 mM in Tris at pH 7.5 or a high concentration of EDTA.

Ionic detergents (e.g., SDS) will interfere with the binding as well as high concentrations of chelating reagents like EDTA, EGTA, and very strong electron donors like metal ions.

To determine the approximate amount of bound His-tagged fusion protein/peptide, a standard curve of a previously purified preparation can be applied.

The detection limit for each protein depends on the assay system used (e.g., primary and secondary antibody, incubation time, detection reagent), the accessibility of the His-tagged fusion biomolecule, and the size of the protein (large proteins bind with a low density). Using a 25 kDa 6xHis-tagged protein, we have observed a detection limit of 1.0 ng per well (100 µL).

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