RED 660™ Protein Assay (22 Citations)
Catalog
Description
Size
Price(USD)
Qty
Catalog
786-676
786-676
Description
RED 660™ Protein Assay
RED 660™ Protein Assay
Size
500 Assays/ 2,500 Micro-assays
500 Assays/ 2,500 Micro-assays
$203.00
$203.00
Catalog
786-899
786-899
Description
RED 660™ Protein Assay with Non Animal Protein Standard
RED 660™ Protein Assay with Non Animal Protein Standard
Size
500 Assays/ 2,500 Micro-assays
500 Assays/ 2,500 Micro-assays
$203.00
$203.00
RED 660™ Protein Assay is a single reagent colorimetric assay that outperforms commercial colorimetric assays, including Bradford and improved Coomassie/ Bradford assays. RED 660™ Protein Assay offers greater linearity, greater color stability, and greater compatibility with detergents, reducing agents and other interfering agents compared to the Coomassie assays. The single, ready-to-use reagent allows for rapid analysis of total protein concentration and generates highly reproducible results.
This assay is suitable for the simple and rapid estimation of protein concentration and detects proteins in the range of 50-2000µg/ml. This assay is based on a single proprietary dye-metal complex reagent. The binding of protein to the dye-metal complex under acidic conditions results in a change of color from reddish-brown to green and this change in color density is proportional to protein concentration. The color change is a result of deprotonation of the dye-metal complex at low pH, which is facilitated by interactions with positively charged amino acid groups. Protein estimation can be performed using as little as 0.5µg protein. The protein-dye complexes reach a stable end point in 5 minutes, remaining stable for several days.
The RED 660™ Protein Assay has sufficient reagents for 500 standard test tube assays or 2,500 standard microwell assays.
This assay is suitable for the simple and rapid estimation of protein concentration and detects proteins in the range of 50-2000µg/ml. This assay is based on a single proprietary dye-metal complex reagent. The binding of protein to the dye-metal complex under acidic conditions results in a change of color from reddish-brown to green and this change in color density is proportional to protein concentration. The color change is a result of deprotonation of the dye-metal complex at low pH, which is facilitated by interactions with positively charged amino acid groups. Protein estimation can be performed using as little as 0.5µg protein. The protein-dye complexes reach a stable end point in 5 minutes, remaining stable for several days.
The RED 660™ Protein Assay has sufficient reagents for 500 standard test tube assays or 2,500 standard microwell assays.
The assay is supplied with a traditional bovine serum albumin (BSA) protein standard or a non animal protein standard.
RED 660™ Protein Assay is compatible with most detergents and its compatibility can be furthered enhanced with Neutralizer™ (See figure 1 below).
INTERFERENCE TO PROTEIN ASSAY
The following table lists the agents compatible with the RED 660 Protein Assay. The table also shows the acceptable concentration of reagents for standard protocols. In most cases, using a correct blank will eliminate or minimize the error caused by interference. * Indicates acceptable concentration when RED 660 Protein Assay Reagent is supplemented with Neutralizer™.
Features
- RAPID: Single reagent assays
- VERSATILE: Compatible with higher range of detergents and reducing agents
- LINEAR: Perfect linear standard curves compared to other protein assays
Applications
- Protein estimation of samples in aqueous buffers
- Estimation in presence of detergents
Protocol | |
786-676 | |
786-899 |
Material Safety Data Sheet | |
786-676 | |
786-899 |
Technical Literature | |
A Non-Animal Alternative to BSA Protein Standards | |
Bioassays Handbook | |
Protein Assay Handbook & Selection Guide | An introduction to protein assays. |
- Bolnick, Daniel I. et al (2023) The dominance of coinfecting parasites' indirect effects on host traits. BIORXIV. https://doi.org/10.1101/2023.02.12.528182
- SchleckerL, L et al (2022) Mechanisms and potential immune tradeoffs of accelerated coral growth induced by microfragmentation. PEERJ. https://doi.org/10.7717/peerj.13158
- Spiers, Jereme G. et al (2021) Hepatic Homeostasis of Metal Ions Following Acute Repeated Stress Exposure in Rats. ANTIOXIDANTS. https://doi.org/10.3390/antiox11010085
- Zhang, X. et al (2019) Normal increases in insulin-stimulated glucose uptake after ex vivo contraction in neuronal nitric oxide synthase mu (nNOSμ) knockout mice. Eur J Physiol. doi.org/10.1007/s00424-019-02268-1
- Chen, H. J. C. et al (2018) Sub-acute restraint stress progressively increases oxidative/nitrosative stress and inflammatory markers while transiently upregulating antioxidant gene expression in the rat hippocampus. Free Radic. Biol. Med.130:446.
- Fyfe, J. et al (2017) Ribosome biogenesis adaptation and mTORC1 signalling in human skeletal muscle following 1 concurrent training compared with resistance training alone. bioRxiv https://doi.org/10.1101/115212
- Goulet, T. et al (20127) The effects of elevated seawater temperatures on Caribbean gorgonian corals and their algal symbionts, Symbiodinium spp.PLoS One doi:10.1371/journal.pone.0171032
- Parker, L. et al (2017) The effect of exercise-intensity on skeletal muscle stress kinase and insulin protein signaling. PLoS One http://dx.doi.org/10.1371/journal.pone.0171613
- Aykul, S. and Martinez-Hackert, E. (2016) Transforming Growth Factor-β Family Ligands Can Function as Antagonists by Competing for Type II Receptor Binding.J. Biol. Chem. 2016; 291:10792-10804.
- Fuess, L. E. et al ( 2016) Associations between transcriptional changes and protein phenotypes provide insights into immune regulation in corals.Dev. Comp. Immunol.doi:10.1016/j.dci.2016.04.017
- Seaman, J.E. et al (2016) Cacidases: caspases can cleave after aspartate, glutamate and phosphoserine residues.Cell Death Differ.doi:10.1038/cdd.2016.62
- Shirur, K.P. et al (2016) Lesion recovery and the bacterial microbiome in two Caribbean gorgonian corals Mar. Biol. doi:10.1007/s00227-016-3008-6
- Betteridge, S. at al (2015) No effect of acute beetroot juice ingestion on oxygen consumption, glucose kinetics or skeletal muscle metabolism during submaximal exercise in males. J. Appl. Physiol. DOI: 10.1152/japplphysiol.00658.2015
- Wallace, R. D. and Bates, E. (2015) Differential Effects of Organic and Inorganic Mercury on Phenotypically Variant Breast Cancer Cell Lines.J Clin Toxicol.5:273
- Chen, H. C. et al (2014) Stress. 17:250
- Mann, W. T. et al (2014) Mar Biol. 161:2213
- Pinzon, J. H. et al (2014) PeerJ. 2:e628
- Pinzon, J. H. et al (2014) PLOS. 9(8): e104787
- Saremirad, P. et al (2014) J. Chroma A. 1359:70
- Saremirad, P. et al (2014) J. Chroma A. 1370:147
- Schaeffer, E.K. et al (2014) Blood Cell Mol. Dis. 52:214
- Spiers, J.G. et al (2014) Chem. Senses. doi: 10.1093/chemse/bju026