Passage Reagent PRG-3 (Trypsin Inhibitor Solution 1X), 100ml
A part of the Passage Reagent Group™ (PRG).
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- PRODUCT INFO
- CITATIONS
- DOCUMENTATION
Gain Consistency with our Single Lot Media and Reagents
The Passage Reagent Group™ (PRG) is a matched set of CSC Certified™ reagents for releasing cells from culture for subculture or freezing. The PRG contains three parts: PRG-1™ (EDTA-dPBS Solution), PRG-2™ (Trypsin/EDTA-dPBS Solution) and PRG-3™(Trypsin Inhibitor-dPBS Solution) The chelating agent EDTA in PRG-1™ prepares for PRG-2™, which contains highly purified trypsin. PRG-3™ inactivates the protease in PRG-2™ and stabilizes the cell membranes.
Cell membranes are materially and cumulatively damaged whenever cells are exposed to serine proteases, physically manipulated, centrifuged, and/or frozen. Use of the PRG greatly minimizes damage and stress to cells during passage or freezing of cell cultures.
PRG-3™ is intended for sequential use with PRG-1™ and PRG-2™. PRG-3™ inhibits the trypsin activity of PRG-2™, preventing nonspecific protease damage to cell membranes after detachment.
Storage and Handling
Store at -20°C. Once opened, shelf life 30 days at +2 - 8°C
Cell Systems media and reagents are made with WFI, all components are cGMP and ISO Compliant, and are classified "Sterile".
A Selection of Citations for Passage Reagent Group™ from Scientific Journals
Discover additional research on Google Scholar that utilizes Cell Systems reagents.
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"Optimization of an in vitro human blood–brain barrier model: Application to blood monocyte transmigration assays" Paradis et al. MethodsX, 2015
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"S100A4 is upregulated in proliferative diabetic retinopathy and correlates with markers of angiogenesis and fibrogenesis" Abu El-Asrar et al. Molecular Vision, 2014
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"Isolation of purified H and L polypeptide chains from guinea-pig gamma-2-immunoglobulin after mild reduction" Lamm et al. Immunology, 2014)
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"Optical Recording Reveals Novel Properties of GSK1016790A-Induced Vanilloid Transient Receptor Potential Channel TRPV4 Activity in Primary Human Endothelial Cells" Sullivan et al. Molecular Pharmacology, 2012
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"High-Glucose-Induced Endothelial Cell Injury Is Inhibited by a Peptide Derived from Human Apolipoprotein E." Bhattacharjee et al. PLOs One, 2012
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"Soluble aggregates of the amyloid-beta are trapped by serum albumin to enhance amyloid-beta activation of endothelial cells" Barcelo et al. Journal of Biological Engineering, 2009
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