Product Description


  • PROTEOSAVE™ series products have a unique high hydrophilic polymer surface treatment.
  • The tube and well surface are coated with a high density hydroxyl group which blocks the non-specific binding of proteins, peptide and cells to the surface dramatically.
  • This effectively prevents your sample loss originated from the non-specific binding to the tube/ plate.

For free samples of ProteoSave™ click here


Exosome Recovery - ProteoSaveComparison study of PROTEOSAVE™ and other low binding tubes for Exosome recovery.

View the Comparison Study

Protein Recovery with PROTEOSAVE Tubes

Collection / Preservation

  • To preserve cell expressed proteins and preparation of culture additives and proteins
  • To reduce loss of protein in a valuable sample

Organic solvent and heat resistant

Cat. NoProductMaterialNoteQty/PkQty/Cs
MS-4205MZPROTEOSAVE 0.5mL MicrotubePolypropyleneNon-sterilized100500
MS-4255MZPROTEOSAVE 0.5mL MicrotubePolypropyleneRadiation sterilized100500
MS-4215MZPROTEOSAVE 1.5mL MicrotubePolypropyleneNon-sterilized100500
MS-4265MZPROTEOSAVE 1.5mL MicrotubePolypropyleneRadiation sterilized100500
MS-4201MZPROTEOSAVE 0.5mL SlimtubePolypropyleneNon-sterilized50500
MS-4202MZPROTEOSAVE 1.5mL SlimtubePolypropyleneNon-sterilized50500


Storage: Room temperature

Expiration: 2 years after production

Operational temperature -80ºC to 40ºC

Cat. NoProductMaterialNoteQty/PkQty/Cs
MS-8296FZPROTEOSAVE 96F PlatePolystyleneNo Lid, radiation sterilized550
MS-8296KZPROTEOSAVE 96F Plate (black)PolystyreneNo Lid, Non-sterilized550
MS-3296UZPROTEOSAVE 96U PlatePolystyreneNo Lid, Non-sterilized550
MS-52150ZPROTEOSAVE 15mL Conicaltube*Body: PET Cap: PolyethyleneNon-sterilized5100
MS-52550ZPROTEOSAVE 50mL Conicaltube*Body: Polypropylene Cap: PolyethyleneRadiation sterilized5100


Storage: Room temperature

Expiration: 2 years after production

*: Operational temperature -80ºC to 40ºC


Temperature rage for use: -80°C-40°C

Upper strength of centrifuge: 4,640G (In-house data: Rotation time 10 min, Use of Swing rotor, rubber)


  • Reduce the adsorption of protein, peptides and cells
  • Resistance to organic solvents, detergents and heat (boiling at 100°C, 10min.)
  • Sterilized products are suitable for the preservation of cell products, additives and freeze

S-BIO ProteoSave™ Product Brochure

Microtube (MS-4205M,MS-4255M,MS-4215M,MS-4265M)】

  1. ARISAKA, Yoshinori, et al. A heparin-modified thermoresponsive surface with heparin-binding epidermal growth factor-like growth factor for maintaining hepatic functions in vitro and harvesting hepatocyte sheets. Regenerative Therapy, 2016, 3: 97-106.
  2. PANDEY, Kiran; NAHAR, Ashrafun; KADOKAWA, Hiroya. Method for isolating pure bovine gonadotrophs from anterior pituitary using magnetic nanoparticles and anti-gonadotropin-releasing hormone receptor antibody. Journal of Veterinary Medical Science, 2016, 78.11: 1699-1702.
  3. HAMAMURA, Kensuke, et al. ANNALS EXPRESS: Simple quantitation for potential serum disease biomarker peptides, primarily identified by a peptidomics approach in the serum with hypertensive disorders of pregnancy. Annals of Clinical Biochemistry: An international journal of biochemistry and laboratory medicine, 2015, 0004563215583697.
  4. IZAKI, Shunsuke, et al. Feasibility of Antibody–Poly (Glutamic Acid) Complexes: Preparation of High‐Concentration Antibody Formulations and Their Pharmaceutical Properties. Journal of pharmaceutical sciences, 2015, 104.6: 1929-1937.
  5. OGISO, Hideo; TANIGUCHI, Makoto; OKAZAKI, Toshiro. Analysis of lipid-composition changes in plasma membrane microdomains. Journal of lipid research, 2015, 56.8: 1594-1605.
  6. ICHIKAWA, Shunsuke, et al. Cellulosomal carbohydrate-binding module from Clostridium josui binds to crystalline and non-crystalline cellulose, and soluble polysaccharides. FEBS letters, 2014.
  7. KADOKAWA, Hiroya, et al. Gonadotropin-releasing hormone (GnRH) receptors of cattle aggregate on the surface of gonadotrophs and are increased by elevated GnRH concentrations. Animal reproduction science, 2014, 150.3: 84-95.
  8. UCHIDA, Yasuo, et al. A study protocol for quantitative targeted absolute proteomics (QTAP) by LC-MS/MS: application for inter-strain differences in protein expression levels of transporters, receptors, claudin-5, and marker proteins at the blood–brain barrier in ddY, FVB, and C57BL/6J mice. Fluids and Barriers of the CNS, 2013, 10.1: 21.
  9. NAGAI, Yutaka; TAKAO, Masashi. Monoclonal antibody to human epithelial cell adhesion molecule and method for detecting circulating tumor cells using the same. U.S. Patent Application 14/085,205, 2013.
  10. TAKAO, Masashi; NAGAI, Yutaka; TORII, Tokiji. Cysteine-Poor Region-Specific EpCAM Monoclonal Antibody Recognizing Native Tumor Cells with High Sensitivity. Monoclonal antibodies in immunodiagnosis and immunotherapy, 2013, 32.2: 73-80.
  11. YASUNO, K., et al. Development of Podocyte Injuries in Osborne–Mendel Rats is Accompanied by Reduced Expression of Podocyte Proteins. Journal of comparative pathology, 2013, 149.2: 280-290.
  12. TSUCHIYA, Hikaru; TANAKA, Keiji; SAEKI, Yasushi. The parallel reaction monitoring method contributes to a highly sensitive polyubiquitin chain quantification. Biochemical and biophysical research communications, 2013, 436.2: 223-229.
  13. KUROKAWA, Kenji, et al. Novel bacterial lipoprotein structures conserved in low-GC content Gram-positive bacteria are recognized by Toll-like receptor 2. Journal of Biological Chemistry, 2012, 287.16: 13170-13181.
  14. UMEMURA, Hiroshi, et al. Identification of a high molecular weight kininogen fragment as a marker for early gastric cancer by serum proteome analysis. Journal of gastroenterology, 2011, 46.5: 577-585.
  15. KAWAKAMI, Hirotaka, et al. Dynamics of absolute amount of nephrin in a single podocyte in puromycin aminonucleoside nephrosis rats calculated by quantitative glomerular proteomics approach with selected reaction monitoring mode. Nephrology Dialysis Transplantation, 2011, gfr492.
  16. TAKAO, Masashi; TAKEDA, Kazuo. Enumeration, characterization, and collection of intact circulating tumor cells by cross contamination‐free flow cytometry. Cytometry Part A, 2011, 79.2: 107-117.
  17. FUKUMOTO, Hiroaki, et al. High-molecular-weight β-amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients. The FASEB Journal, 2010, 24.8: 2716-2726.


  1. ICHIKAWA, S.; KARITA, S. Characterization of Family 3 Carbohydrate-binding Module from Clostridium josui. In: Proceedings of the Second International Workshop on Regional Innovation Studies:(IWRIS2010). Graduate School of Regional Innovation Studies, Mie University, 2010. p. 5-8.


Conical tube (MS-52150,MS-52550)】

  1. YOSHIMOTO, Shogo, et al. An Acinetobacter trimeric autotransporter adhesin reaped from cells exhibits its nonspecific stickiness via a highly stable 3D structure. Scientific Reports, 2016, 6.
  2. HATTORI, Kotaro, et al. Increased cerebrospinal fluid fibrinogen in major depressive disorder. Scientific reports, 2015, 5: 11412.
  3. WATANABE, H., et al. Controlled release of a protein using a ceramic carrier and zinc ions as a novel approach to the treatment of osteoporosis. In: Key Engineering Materials. 2015. p. 332-337.
  4. IHARA, Yuta; OHTA, Hiroyuki; MASUDA, Shinji. A highly sensitive quantification method for the accumulation of alarmone ppGpp in Arabidopsis thaliana using UPLC-ESI-qMS/MS. Journal of plant research, 2015, 128.3: 511-518.
  5. KIM, Jong-Myong, et al. Highly Reproducible ChIP-on-Chip Analysis to Identify Genome-Wide Protein Binding and Chromatin Status in Arabidopsis thaliana. In: Arabidopsis Protocols. Humana Press, 2014. p. 405-426.


96F Plate (MS-8296F)】

  1. FUKAZAWA, Tominaga; YAMAZAKI, Yuri; MIYAMOTO, Yohei. Reduction of non-specific adsorption of drugs to plastic containers used in bioassays or analyses. Journal of pharmacological and toxicological methods, 2010, 61.3: 329-333.


96F Plate, Black (MS-8296K)】

  1. ANDOU, Takashi, et al. RNA detection using peptide-inserted Renilla luciferase. Analytical and bioanalytical chemistry, 2009, 393.2: 661-668.



  1. KUBOTA, Hiroyuki, et al. Reduction in IgE reactivity of Pacific mackerel parvalbumin by heat treatment. Food chemistry, 2016, 206: 78-84.
  2. KASUGA, Kie. Comprehensive analysis of MHC ligands in clinical material by immunoaffinity-mass spectrometry. In: The Low Molecular Weight Proteome. Springer New York, 2013. p. 203-218.
  3. YAMASHITA, Kazuyuki; SHIROKI, Masahiro. Medical or biochemical resin composition and resin molded product. U.S. Patent Application 13/469,768, 2012.
  4. GOTOH, Akiko, et al. Evaluation of adsorption of urine cystatin C to the polymer materials on the microplate by an antigen capture enzyme-linked immunosorbent assay. Clinica Chimica Acta, 2008, 397.1: 13-17.

Available Options

Catalog No.CapacitySterilizationMaterialQty Per CasePriceQuantity
#MS-82962RDeep Well, 96V RNon-sterilizedPolypropylene15 per case$606.00
#MS-4205MZ.5mL MicrotubeNon-sterilizedPolypropylene500 per case$230.00
#MS-4215MZ1.5mL MicrotubeNon-sterilizedPolypropylene500 per case$200.00
#MS-4255MZ.5mL MicrotubeRadiation sterilizedPolypropylene500 per case$260.00
#MS-4265MZ1.5mL MicrotubeRadiation sterilizedPolypropylene500 per case$230.00
#MS-52150Z15mL Conicaltube*Non-sterilizedPolypropylene100 per case$311.00
#MS-52550Z50mL Conicaltube*Radiation sterilizedPolypropylene100 per case$311.00
#MS-3296UZ96U Plate, No LidNon-sterilizedPolypropylene50 per case$417.00
#MS-8296FZ96F Plate, No LidNon-sterilizedPolystylene50 per case$417.00
#MS-4201XZ.5mL SlimtubeNon-sterilizedPolypropylene500 per case$635.00
#MS-4202XZ1.5mL SlimtubeNon-sterilizedPolypropylene500 per case$635.00
#MS-8296VZ96V Plate, No LidNon-sterilizedPolystylene20 per case$254.00