住友ベークライト　プロテオセーブ^®

貴重なサンプル（タンパク質、ペプチド、低分子化合物など）の濃度調整や保管時のロスを低減

　光架橋超親水性ポリマーを用いて基材表面を均一に処理することで、親水化表面を形成します。これにより、タンパク質やペプチドの非特異的吸着を抑制し、試料の損失を低減します。
　また、基材とポリマーは化学的に結合しているため、容器からのポリマーの溶出も心配ありません。

耐有機溶媒性と耐熱性も大幅UP*

光架橋による基材との共有結合によるコーティングにより、従来のコーティングでは困難であった耐有機溶剤性と耐熱性も保たれています。
*対応製品：材質がポリプロピレンの製品(マイクロチューブ、スリムチューブ、50 mL遠沈管、96Vプレート、96Vディープウェルプレート)

真菌胞子の分析での使用例

粘性が強い真菌胞子（炭疽病菌胞子）を用いて回収率を比較したところ、プロテオセーブ^®は一般遠沈管に比べ回収率が向上した。

エクソソームの分析での使用例

PC-3細胞由来の精製エクソソームを用いて他社低吸着製品とCD63シグナル量を比較したところ、プロテオセーブ^®はエクソソームの吸着が少なく、移し替え前とほぼ同じシグナルが得られた。

プロテオミクスでの使用例

肝がん細胞Hep3B由来のペプチドを用いてLC-MSにおける他社低吸着製品とのペプチド同定数を比較したところ、プロテオセーブ^®はペプチド同定数が一番多かった。

低分子化合物の分析での使用例

容器への吸着が多い非イオン性の低分子化合物を用いて容器への吸着を比較したところ、プロテオセーブ^®はノンコート品に比べ吸着を抑制した。

酵素反応実験での使用例

糖転移酵素Endo-Mの加水分解反応実験で他社品と比較したところ、プロテオセーブ^®が反応効率が一番良かった。

耐有機溶剤性・耐熱性／耐寒性

タンパク質構造解析で主に使用される条件下で強い耐性を有することを確認した。

アプリケーション詳細

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Mass spectrometry

1. Mizui, T., et al. (2019). Cerebrospinal fluid BDNF pro-peptide levels in major depressive disorder and schizophrenia. Journal of Psychiatric Research, 113, 190-198.
   https://www.sciencedirect.com/science/article/abs/pii/S0022395618312196?via%3Dihub
2. Igarashi, N., et al. (2018). Increased aqueous autotaxin and lysophosphatidic acid levels are potential prognostic factors after trabeculectomy in different types of glaucoma. Scientific Reports, 8(1), 1-13.
   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6063955/pdf/41598_2018_Article_29649.pdf
3. Hamamura, K., et al. (2015). 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. Advance online publication.
   https://journals.sagepub.com/doi/full/10.1177/0004563215583697
4. Ogiso, H., Taniguchi, M., & Okazaki, T. (2015). Analysis of lipid-composition changes in plasma membrane microdomains. Journal of Lipid Research, 56(8), 1594-1605.
   https://www.jlr.org/content/56/8/1594.short
5. Ihara, Y., Ohta, H., & Masuda, S. (2015). A highly sensitive quantification method for the accumulation of alarmone ppGpp in Arabidopsis thaliana using UPLC-ESI-qMS/MS. Journal of Plant Research, 128(3), 511-518.
   https://link.springer.com/article/10.1007/s10265-015-0711-1
6. Uchida, Y., et al. (2013). 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, 10(1), 21.
   https://fluidsbarrierscns.biomedcentral.com/articles/10.1186/2045-8118-10-21
7. Tsuchiya, H., Tanaka, K., & Saeki, Y. (2013). The parallel reaction monitoring method contributes to a highly sensitive polyubiquitin chain quantification. Biochemical and Biophysical Research Communications, 436(2), 223-229.
   https://www.researchgate.net/publication/237003100_The_parallel_reaction_monitoring_method_contributes_to_a_highly_sensitive_polyubiquitin_chain_quantification/link/00b4952952d2c540c3000000/download
8. Kasuga, K. (2013). Comprehensive analysis of MHC ligands in clinical material by immunoaffinity-mass spectrometry. In The Low Molecular Weight Proteome (pp. 203-218). Springer New York.
   https://dx.doi.org/10.1007/978-1-4614-7209-4_14
9. Umemura, H., et al. (2011). Identification of a high molecular weight kininogen fragment as a marker for early gastric cancer by serum proteome analysis. Journal of Gastroenterology, 46(5), 577-585.
   https://link.springer.com/article/10.1007/s00535-010-0369-3
10. Kawakami, H., et al. (2011). 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. Advance online publication.
    https://academic.oup.com/ndt/article/27/4/1324/1832322

Purification and Analysis of Proteins

1. Sameshima-Yamashita, Y., et al. (2019). Construction of a Pseudozyma antarctica strain without foreign DNA sequences (self-cloning strain) for high yield production of a biodegradable plastic-degrading enzyme. Bioscience, Biotechnology, and Biochemistry, 83(8), 1547-1556.
   https://www.tandfonline.com/doi/full/10.1080/09168451.2019.1571898
2. Honjo, M., et al. (2018). Autotaxin–lysophosphatidic acid pathway in intraocular pressure regulation and glaucoma subtypes. Investigative Ophthalmology & Visual Science, 59(2), 693-701.
   https://iovs.arvojournals.org/article.aspx?articleid=2671878
   Ishii, T., et al. (2018). Increased cerebrospinal fluid complement C5 levels in major depressive disorder and schizophrenia. Biochemical and Biophysical Research Communications, 497(2), 683-688.
   https://www.sciencedirect.com/science/article/abs/pii/S0006291X18303620?via%3Dihub
3. Matsumura, T., et al. (2018). Venom and Antivenom of the Redback Spider (Latrodectus hasseltii) in Japan. Part I. Venom Extraction, Preparation, and Laboratory Testing. Japanese Journal of Infectious Diseases, 71(2), 116-121.
   https://pdfs.semanticscholar.org/659d/ee88c29d09a2d95792b144e28afd353da848.pdf
4. Kinoshita, S., et al. (2018). Injection of cultured cells with a ROCK inhibitor for bullous keratopathy. New England Journal of Medicine, 378(11), 995-1003.
   https://www.nejm.org/doi/full/10.1056/NEJMoa1712770
5. Kobayashi, J., et al. (2018). Effect of temperature changes on serum protein adsorption on thermoresponsive cell-culture surfaces monitored by a quartz crystal microbalance with dissipation. International Journal of Molecular Sciences, 19(5), 1516.
   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5983614/
6. Hidese, S., et al. (2017). Cerebrospinal fluid neural cell adhesion molecule levels and their correlation with clinical variables in patients with schizophrenia, bipolar disorder, and major depressive disorder. Progress in Neuro-Psychopharmacology and Biological Psychiatry, 76, 12-18.
   https://www.sciencedirect.com/science/article/abs/pii/S0278584616301890?via%3Dihub
7. Obayashi, Y., Wei Bong, C., & Suzuki, S. (2017). Methodological considerations and comparisons of measurement results for extracellular proteolytic enzyme activities in seawater. Frontiers in Microbiology, 8, 1952.
   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5641328/
8. Arisaka, Y., et al. (2016). 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, 3, 97-106.
   https://www.sciencedirect.com/science/article/pii/S2352320416000262

Comparison of Products

1. Fukazawa, T., Yamazaki, Y., & Miyamoto, Y. (2010). Reduction of non-specific adsorption of drugs to plastic containers used in bioassays or analyses. Journal of Pharmacological and Toxicological Methods, 61(3), 329-333.
   https://linkinghub.elsevier.com/retrieve/pii/S1056-8719(10)00002-X

General purification & assays

1. Ohara, Y., Yoshimoto, S., & Hori, K. (2019). Control of AtaA-mediated bacterial immobilization by casein hydrolysates. Journal of Bioscience and Bioengineering, 128(5), 544-550.
   https://www.sciencedirect.com/science/article/abs/pii/S1389172319302786?via%3Dihub
2. Yoshida, M., et al. (2018). Preferential capture of EpCAM‐expressing extracellular vesicles on solid surfaces coated with an aptamer‐conjugated zwitterionic polymer. Biotechnology and Bioengineering, 115(3), 536-544.
   http://ir.tdc.ac.jp/irucaa/bitstream/10130/4837/1/bit.26489.pdf
3. 市川 俊輔. (2016). Engineering of a Cellulolytic Bacterium and a Lignocellulose-degrading Enzyme for Utilization of Cellulosic Biomass. PhD Thesis, 三重大学.
   https://mie-u.repo.nii.ac.jp/?action=repository_action_common_download&item_id=10822&item_no=1&attribute_id=17&file_no=1
4. Takao, M., & Takeda, K. (2011). Enumeration, characterization, and collection of intact circulating tumor cells by cross contamination‐free flow cytometry. Cytometry Part A, 79(2), 107-117.
   URL: https://onlinelibrary.wiley.com/doi/epdf/10.1002/cyto.a.21014
5. Ichikawa, S., & Karita, S. (2010). Characterization of Family 3 Carbohydrate-binding Module from Clostridium josui. In Proceedings of the Second International Workshop on Regional Innovation Studies: (IWRIS2010) (pp. 5-8). Graduate School of Regional Innovation Studies, Mie University.
   https://mie-u.repo.nii.ac.jp/?action=pages_view_main&active_action=repository_view_main_item_detail&item_id=6428&item_no=1&page_id=13&block_id=21
6. Andou, T., et al. (2009). RNA detection using peptide-inserted Renilla luciferase. Analytical and Bioanalytical Chemistry, 393(2), 661-668.
   https://link.springer.com/article/10.1007%2Fs00216-008-2473-2