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PROTEOSTAT® Protein aggregation assay

Quantitative Detection of Protein Aggregates from Visible to Subvisible Particles
ENZ-51023-KP050 50 tests 181.00 USD
ENZ-51023-KP002 2x96 tests 485.00 USD
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  • A simple, sensitive, homogenous fluorescent assay
  • Validated for use with microplate or flow cytometry platform
  • Extensively benchmarked with IgG
  • Optimize buffers and excipients for protein formulation
  • Performs with a wide pH and ionic strength range
  • Use with PROTEOSTAT® Protein Aggregation Standards for accurate quantification of aggregated protein in solution.
PROTEOSTAT® Protein aggregation assay provides a simple,  homogenous assay format for monitoring peptide and protein aggregation in solution. This is useful for defining optimal storage formulations for proteins, for screening of compounds that promote or inhibit protein aggregation and potentially for the sensitive measurement of molecular chaperone activity. The assay can be employed to streamline protein processing and formulation optimization procedures. Relative to conventional protein aggregation detection dyes, such as Thioflavin T, the Enzo PROTEOSTAT® detection reagent can detect aggregates from a broader range of proteins, yields a much brighter signal, provides at least 2 orders of magnitude linear dynamic range and offers superior performance across a broad range of pH values (4~10) and buffer compositions. Sensitivity for this assay is in the sub-micromolar range and as little as 1-5% protein aggregate is detectable in a concentrated protein solution. The assay is capable of providing quantitative analysis of protein aggregation in a robust and high-throughput fashion (Z’ factor score >0.5). Lyophilized native and aggregated protein are provided as negative and positive controls for monitoring changes in protein aggregation status.

PROTEOSTAT® Protein Aggregation Standards kit (Prod. No. ENZ-51039) is the only commercially available protein aggregation standards assay with stabilized, high-quality reference samples for generating trace protein aggregate levels in concentrated monomeric IgG.
Easy to use - simply add water!
ENZ-51023 Flow web
Figure 2. Flow Cytometry Application: PROTEOSTAT® Dye Mixed with Bodipy Dye (Pyrromethene 546) Differentiates Oil Droplets From True Protein Aggregates. Bodipy vs PROTEOSTAT® fluorescence of IgG aggregates (A), Silicon oil droplets (B) and a mixture of Silicon oil droplets and IgG aggregates (C).
ENZ-51023 Fig2
ENZ-51023 Fig1

ENZ-51023 Thioflavin T-Structure
Thioflavin T: early prototype dye in the design of PROTEOSTAT® assay which also rotates around a single bond (red arrow) in the absence of protein aggregates.
ENZ-51023 dye aggregate
Dye is immobilized when bound to the aggregate and begins to fluoresce.
ENZ-51023 Fig3U
Effective linear dynamic range for antibody aggregate detection using PROTEOSTAT® Detection Reagent compared with Thioflavin T. Relative fluorescence unit values (RFUs) may differ depending upon the microplate reader employed for the analysis.
Please mouse over
ENZ-51023 Flow web ENZ-51023 Fig2 ENZ-51023 Fig1 ENZ-51023 Thioflavin T-Structure ENZ-51023 dye aggregate ENZ-51023 Fig3U

Product Specification

Applications:Flow Cytometry, Fluorescence microscopy, Fluorescent detection
Application Notes:This kit has been specifically designed for monitoring of protein aggregate formation in solution.
Quality Control:A sample of PROTEOSTAT® Protein aggregation assay was used to assay (1) 20 µM aggregated lysozyme, (2) 20 µM native lysozyme; and (3) mixtures of 5% aggregate. The Z’ factor is greater than 0.5 and the 5% aggregate signal is greater than 3 standard deviations above the no-aggregate control.
Quantity:For ENZ-51023-KP050: 50 tests in a 96 well plate or 16 flow cytometry tests
For ENZ-51023-KP002: 2 x 96-well tests or 70 flow cytometry tests
Use/Stability:With proper storage, the kit components are stable up to the date noted on the product label. Store kit at -20°C in a non-frost free freezer or -80°C for longer term storage.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Contents:PROTEOSTAT® detection reagent
PROTEOSTAT® positive control
PROTEOSTAT® negative control
10X PROTEOSTAT® assay buffer
Technical Info/Product Notes:Application Notes:
Rapid Detection and Characterization of Protein Aggregates by Flow Cytometry

Particle analysis of therapeutic protein formulations with ImageStreamX® Imaging Flow Cytometry and the PROTEOSTAT® Protein Aggregation Assay

Prediction of Aggregation Propensity and Monitoring of Aggregation of Antibody-Drug Conjugates (ADC) using ProteoStat® Reagents

Enzo and PROTEOSTAT are trademarks of Enzo Life Sciences, Inc. Several of Enzo’s products and product applications are covered by US and foreign patents and patents pending.

Product Literature References

Fibril formation and therapeutic targeting of amyloid-like structures in a yeast model of adenine accumulation: D. Laor, et al.; Nat. Commun. 10, 62 (2019), Abstract; Full Text
Caffeic acid and resveratrol ameliorate cellular damage in cell and Drosophila models of spinocerebellar ataxia type 3 through upregulation of Nrf2 pathway: Y.L. Wu, et al.; Free Radic. Biol. Med. 115, 309 (2018), Abstract;
High Throughput Differential Scanning Fluorimetry (DSF) Formulation Screening with Complementary Dyes to Assess Protein Unfolding and Aggregation in Presence of Surfactants: S.M. McClure, et al.; Pharm. Res. 35, 81 (2018), Abstract;
The catalytic inactivation of the N-half of human hexokinase 2 and structural and biochemical characterization of its mitochondrial conformation: M.H. Nawaz, et al.; BioSci. Rep. 38, BSR20171666 (2018), Application(s): Aggregation propensity assessed by DSF, Abstract; Full Text
Trans ε-viniferin is an amyloid-β disaggregating and anti-inflammatory drug in a mouse primary cellular model of Alzheimer's disease: E. Vion, et al.; Mol. Cell. Neurosci. 88, 1 (2017), Abstract;
ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation: J.H. Seo, et al.; Nat. Commun. 7, 12882 (2016), Application(s): , Abstract; Full Text
BRG1 and BRM SWI/SNF ATPases redundantly maintain cardiomyocyte homeostasis by regulating cardiomyocyte mitophagy and mitochondrial dynamics in vivo: S.J. Bultman, et al.; Cardiovasc. Pathol. 25, 258 (2016), Abstract;
Interfacial dilatational deformation accelerates particle formation in monoclonal antibody solutions: G.L. Lin, et al.; Soft Matter 12, 3293 (2016), Abstract;
A screening methodology for purifying proteins with aggregation problems: M. Lebendiker, et al.; Methods Mol. Biol. 1258, 261 (2015), Abstract;
Effects of tau domain-specific antibodies and intravenous immunoglobulin on tau aggregation and aggregate degradation: J.O. Esteves-Villanueva, et al.; Biochemistry 54, 293 (2015), Abstract;
Metal-mediated protein oxidation: applications of a modified ELISA-based carbonyl detection assay for complex proteins: H. Uehara, et al.; Pharm. Res. 32, 691 (2015), Application(s): Effects of metal-mediated protein oxidation on aggregation, Abstract;
WALTZ-DB: a benchmark database of amyloidogenic hexapeptides: J. Beerten, et al.; Bioinformatics 31, 1698 (2015), Abstract;
Amyloid-beta (Aβ1-42)-induced paralysis in Caenorhabditis elegans is reduced by restricted cholesterol supply: C. Regitz, et al.; Neurosci. Lett. 576, 93 (2014), Abstract;
Human Stefin B Role in Cell's Response to Misfolded Proteins and Autophagy: M. Polajnar, et al.; PLoS One 9, e102500 (2014), Application(s): Proteins aggregation and oxidative stress in stefin B KO astrocytes, Abstract; Full Text
Lysosomal enzyme cathepsin B enhances the aggregate forming activity of exogenous α-synuclein fibrils: A. Tsujimura, et al.; Neurobiol. Dis. 73C, 244 (2014), Application(s): In vitro formation of a-synuclein fibrils and monitoring with ProteoStat® dye, Abstract;
ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli: S.Navarro & S.Ventura; Biotechnol. J 9, 1259 (2014), Abstract;
Increased carbonylation, protein aggregation and apoptosis in the spinal cord of mice with experimental autoimmune encephalomyelitis: A. Dasgupta, et al.; ASN Neuro 5, e00111 (2013), Application(s): Detection of protein aggregation in tissue section using fluorescence microscopy, Abstract; Full Text
Optimization of protein purification and characterization using Thermofluor screens: S. Boivin, et al.; Protein Expr. Pur. 91, 192 (2013), Abstract;
Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness: S. Bershtein, et al.; Mol. Cell. 49, 133 (2013), Application(s): Propensity to aggregate for dihydrofolate reductase mutants, Abstract;
Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function: W.M. Rabeh, et al.; Cell 148, 150 (2012), Application(s): Aggregation of multi-domain protein: NBD1, Abstract; Full Text
Detection of α-synuclein amyloidogenic aggregates in vitro and in cells using light-switching dipyridophenazine ruthenium(II) complexes: N.P. Cook, et al.; J. Am. Chem. Soc. 134, 20776 (2012), Abstract;
p62/SQSTM1-Dependent Autophagy of Lewy Body-Like α-Synuclein Inclusions: Y. Watanabe, et al.; PLoS One 7, e52868 (2012), Application(s): Protein aggregation of alpha-synuclein, Abstract; Full Text
Raster image correlation spectroscopy as a novel tool for the quantitative assessment of protein diffusional behaviour in solution: Z. Hamrang, et al.; J. Pharm. Sci. 101, 2082 (2012), Abstract;
High sensitivity luminescence nanoparticle assay for the detection of protein aggregation: S. Pihlasalo, et al.; Anal. Chem. 83, 1163 (2011), Abstract;

General Literature References

Emerging analytical technologies for biotherapeutics development: R. Krishnamurthy et al.; Bioprocess International 6 (5), 32 (2008),
Aggregation analysis of therapeutic proteins, part 2: T. Arakawa et al.; Bioprocess International 5 (4), 36 (2007),
Aggregation analysis of therapeutic proteins, part 3: T. Arakawa et al.; Bioprocess International 5(10), 52 (2007),
Aggregation analysis of therapeutic proteins, part 1: T. Arakawa, et al.; Bioprocess International 4 (10), 32 (2006),
Structure of the cross-beta spine of amyloid-like fibrils: R. Nelson et al.; Nature 435, 773 (2005), Abstract;

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