Tris Resuspension

Tris resuspension is the process of dispersing a biological pellet or concentrated sample in a Tris-based buffer, a routine step that prepares material for downstream analysis. Tris, or tris(hydroxymethyl)aminomethane, helps maintain a stable pH, while pipetting, gentle vortexing, or repeated mixing breaks up the pellet and distributes its components throughout the solution. In biology, this approach supports the handling of nucleic acids, proteins, and other cellular materials before procedures such as extraction, electrophoresis, enzymatic reactions, or spectroscopic measurements. Consistent resuspension improves sample homogeneity, reduces material loss, and promotes reproducible experimental results.

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Research

JoVE Journal - Biology

Western Blotting Using the Invitrogen NuPage Novex Bis Tris MiniGels

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Cited by 28 •

2007

This technical article describes a standard western-blotting procedure using the commercially available NuPAGE electrophoresis Mini-Gel system from Invitrogen.

An In Vitro Enzymatic Assay to Measure Transcription Inhibition by Gallium(III) and H3 5,10,15-tris(pentafluorophenyl)corroles

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Cited by 1 •

2015

Gallium(III) 5,10,15-(tris)pentafluorophenylcorrole and its freebase analogue exhibit low micromolar cell cytotoxicity. This manuscript describes an RNA transcription reaction, imaging RNA with an ethidium bromide-stained gel, and quantifying RNA with UV-Vis spectroscopy, in order to assess transcription inhibition by corroles and demonstrates a straightforward method of evaluating anticancer candidate properties.

Selective Purification of a Bacterial Protein by Negative Ion-Exchange Chromatography

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2025

Source: Kuo, T., et al. One-step Negative Chromatographic Purification of Helicobacter pylori Neutrophil-activating Protein Overexpressed in Escherichia coli in Batch Mode. J. Vis. Exp. (2016)The video demonstrates a negative chromatography technique to purify a virulence-associated protein from a bacterial lysate. By using a positively charged resin in a buffered solution, host-cell proteins are selectively retained, while the near-neutral target protein remains unbound and is collected in the...

One-step Negative Chromatographic Purification of Helicobacter pylori Neutrophil-activating Protein Overexpressed in Escherichia coli in Batch Mode

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Cited by 2 •

2016

A high yield method for one-step negative purification of recombinant Helicobacter pylori neutrophil-activating protein (HP-NAP) overexpressed in Escherichia coli by using diethylaminoethyl resins in batch mode is described. HP-NAP purified by this method is beneficial for the development of vaccines, drugs, or diagnostics for H. pylori-associated diseases.

RNA-Protein Pull-Down Assay to Isolate RNA-Binding Proteins via Affinity Extraction

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2025

This video demonstrates an in vitro RNA pull-down assay to identify RNA-binding proteins (RBPs), which interact with the adenylate-uridylate-rich element (ARE) sequences in mRNA. The target RBPs from a cell lysate are mixed with an RNA probe to form RNA-protein complexes. The complexes are isolated via affinity purification utilizing the affinity of the desthiobiotin label of the RNA probe to a streptavidin-labeled magnetic bead.

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