| Field | Specification |
|---|---|
| Mfr No | |
| Assay Time | |
| Detection Method | |
| Product Type | |
| Sample Type(s) | Biological, environment, food, and beverage |
| Shipping | |
| Species | |
| Storage |
Overview
For quantitative determination of copper(II) ion and evaluation of drug effects on Cu metabolism. The assay uses OD359nm for signal readout. Compatible sample input includes Biological, environment, food, and beverage. Typical stated assay timing is 10 min.
Key elements and design rationale
- Readout format: OD359nm supports plate-based signal acquisition and consistent comparison across matched samples.
- Sample compatibility: The stated sample scope includes Biological, environment, food, and beverage, which is useful when aligning matrix type with calibration and control design.
- Analytical range context: The supplied specifications include a stated detection limit of 7 µg/dL (1.0 µM) for interpreting low-signal samples.
- Feature emphasis: Sensitive and accurate. Linear detection range 7 µg/dL (1.0 µM) to 300 µg/dL (47 µM) copper in a 96-well plate assay.
Additional feature notes highlight Simple and high-throughput. The simple procedure can be readily automated as a high-throughput assay in 96-well plates for thousands of samples per day; Improved reagent stability and versatility. The optimized formulation has greatly enhanced the reagent and signal stability. Cuvet or 96-well plate assay. Available format information for this listing includes 250 Tests.
Biological background
This product is centered on measurement of copper within the matrices described for the assay. In practice, datasets from this type of format are typically interpreted by comparing relative signal, activity, or abundance across matched control and experimental groups rather than relying on a single value in isolation. Careful alignment of sample matrix, incubation window, and calibration strategy is important when comparing results across plates, operators, or study days.
More details
Copper is an essential trace element. Copper-containing enzymes play important roles in iron and catecholamine metabolism, free radical scavenging, and in the synthesis of hemoglobin, elastin, and collagen. Copper is mainly present in caeruloplasmin in the liver. Low levels of copper have been associated with mental retardation, depigmentation, anemia, hypotonia, and scorbutic changes in bone. Levels of copper are a key diagnostic indicator of diseases such as Wilson’s disease, microcytic hypochromic anemia, and bone disease due to reduced collagen synthesis. Simple, direct, and automation-ready procedures for measuring copper concentrations find wide applications in research, drug discovery, and environmental monitoring. BioAssay Systems copper assay kit is designed to measure copper with no or minimal sample treatment. The improved method utilizes a chromogen that forms a colored complex specifically with copper ions. The intensity of the color, measured at 359nm, is directly proportional to the copper concentration in the sample. The optimized formulation substantially reduces interference by substances in the raw samples.
Detection method
Colorimetric (OD 359 nm).
Detection limit and analytical sensitivity
Reported detection limit: 7 µg/dL (1.0 µM).
Procedures and timing
Stated procedure or timing information: 10 min.
Research relevance and current trends
- Plate-based quantification and side-by-side group comparison remain central use cases for this assay format.
- The product notes emphasize multi-sample throughput, making it relevant for screening-oriented and larger batch comparison studies.
- The description supports intervention-focused study designs in which researchers compare baseline and perturbed conditions.
Common research applications
- Quantify copper in biological, environment, food, and beverage by OD359 nm readout.
- Compare treatment or phenotype groups using matched biological, environment, food, and beverage handling.
- Monitor time-course or pre/post changes in biological, environment, food, and beverage across study conditions.
Interpretation is usually strongest when signal changes are assessed alongside matrix-matched controls, replicate agreement, and the assay's stated analytical window.
Notes for experimental interpretation
- Matrix composition, background signal, and sample handling can influence apparent response; compare like-with-like whenever possible.
- Use appropriate blanks, controls, and replicate wells to distinguish biological differences from plate, reagent, or handling variability.
For laboratories requiring additional technical capacity, we provide scientific support services including assay execution, method guidance, product sourcing, and customization to align the assay with specific experimental objectives. If you need assistance selecting the appropriate kit configuration, adapting the workflow to your application, or identifying related research services, please click Talk to a Scientist, email support@biohippo.com, or review our Research Services; a member of our scientific team will follow up with recommendations tailored to your study.
Extracellular vesicles promote transkingdom nutrient transfer during viral-bacterial co-infection
Hendricks, M. R., et al (2021). Extracellular vesicles promote transkingdom nutrient transfer during viral-bacterial co-infection. Cell Reports, 34(4), 108672. Assay: Copper in bacteria media.
Maternal perinatal transfer of vitamins and trace elements to piglets
Matte, J. J., & Audet, I. (2020). Maternal perinatal transfer of vitamins and trace elements to piglets. Animal: An International Journal of Animal Bioscience, 14(1), 31-38. Assay: Copper in pig serum.
A fungal ascorbate oxidase with unexpected laccase activity
Braunschmid, V., et al. (2020). A fungal ascorbate oxidase with unexpected laccase activity. International Journal of Molecular Sciences, 21(16). Assay: Copper in yeast cells.
72-Hour in vivo evaluation of nitric oxide generating artificial lung gas exchange fibers in sheep
Lai, A., et al. (2019). 72-Hour in vivo evaluation of nitric oxide generating artificial lung gas exchange fibers in sheep. Acta Biomaterialia, 90, 122-131. Assay: Copper in sheep tissue and serum.
In vivo [64Cu] CuCl2 PET imaging reveals activity of Dextran-Catechin on tumor copper homeostasis
Parmar, A., Pascali, G., Lerra, L., Yee, E., Ahmed-Cox, A., Kimpton, K. & Liu, G. J. (2018). In vivo [64Cu] CuCl2 PET imaging reveals activity of Dextran-Catechin on tumor copper homeostasis. Theranostics, 8(20), 5645-5659. Assay: Copper in neuroblastoma cell.
Estimating global enzyme abundance levels from cofactor requirements: a model-based analysis of the iron metabolism in yeast
Dikicioglu, D., & Oliver, S. G. (2017). Estimating global enzyme abundance levels from cofactor requirements: a model-based analysis of the iron metabolism in yeast. bioRxiv, 229104. Assay: Copper in S. cerevisiae cells.
Dextran-Catechin inhibits angiogenesis by disrupting copper homeostasis in endothelial cells
Yee, E. M., Brandl, M. B., Pasquier, E., Cirillo, G., Kimpton, K., Kavallaris, M. & Vittorio, O. (2017). Dextran-Catechin inhibits angiogenesis by disrupting copper homeostasis in endothelial cells. Scientific reports, 7(1), 7638. Assay: Copper in human cells.
Dextran-Catechin: An anticancer chemically-modified natural compound targeting copper that attenuates neuroblastoma growth
Vittorio, O., Brandl, M., Cirillo, G., Kimpton, K., Hinde, E., Gaus, K. & Haber, M. (2016). Dextran-Catechin: An anticancer chemically-modified natural compound targeting copper that attenuates neuroblastoma growth. Oncotarget 7(30): 47479-47493. Assay: Copper in human cells.
Selected Biochemical Indicators of Equine Rhabdomyolysis in Arabian Horses: Acute Phase Proteins and Trace Elements
EL-Deeb, W. M., & El-Bahr, S. M. (2014). Selected Biochemical Indicators of Equine Rhabdomyolysis in Arabian Horses: Acute Phase Proteins and Trace Elements. Journal of Equine Veterinary Science 34(4): 484-488. Assay: Copper in horse serum.
Bartnikas TB (2012) Known and potential roles of transferrin in iron biology. Biometals 25(4):677-86. Assay: Copper in h
Bartnikas TB (2012) Known and potential roles of transferrin in iron biology. Biometals 25(4):677-86. Assay: Copper in human protein.
Philips N et al (2012) Beneficial regulation of fibrillar collagens, heat shock protein-47, elastin fiber components, tr
Philips N et al (2012) Beneficial regulation of fibrillar collagens, heat shock protein-47, elastin fiber components, transforming growth factor-beta1, vascular endothelial growth factor and oxidative stress effects by copper in dermal fibroblasts. Connect Tissue Res. 53(5):373-8. Assay: Copper in human cell.
Piret JP et al (2012) Differential toxicity of copper (II) oxide nanoparticles of similar hydrodynamic diameter on human
Piret JP et al (2012) Differential toxicity of copper (II) oxide nanoparticles of similar hydrodynamic diameter on human differentiated intestinal Caco-2 cell monolayers is correlated in part to copper release and shape. Nanotoxicology 6:789-803. Assay: Copper in human cell.
Copper (II) oxide nanoparticles penetrate into HepG2 cells, exert cytotoxicity via oxidative stress and induce pro-inflammatory response
Piret, JP et al (2012). Copper (II) oxide nanoparticles penetrate into HepG2 cells, exert cytotoxicity via oxidative stress and induce pro-inflammatory response. Nanoscale 4(22): 7168-7184. Assay: Copper in human cell culture medium.
Plasma biomarkers in pediatric patients undergoing cardiopulmonary bypass
Lull ME, et al (2008). Plasma biomarkers in pediatric patients undergoing cardiopulmonary bypass. Pediatr Res. 63(6):638-44. Assay: Copper in human plasma.