Tris-hcl Resuspension

Tris-HCl resuspension is the process of redistributing a biological sample in Tris-HCl buffer after centrifugation or storage, restoring uniform access to a controlled aqueous environment. Tris maintains pH through reversible proton acceptance and release by the Tris base, while hydrochloric acid sets the buffer pH; thorough mixing breaks up pellets without necessarily disrupting their molecular contents. In molecular and cell biology, this step supports recovery of bacterial or cultured-cell pellets, nucleic acid preparations, and protein samples before lysis, purification, quantification, or downstream analysis. It improves sample homogeneity and reproducibility, although buffer pH and concentration should match the stability requirements of the target material.

Tris-hcl Resuspension - Related Videos

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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.

Determination of the Glycogen Content in Cyanobacteria

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Cited by 26 •

2017

Here, we present a reliable and easy assay to measure the glycogen content in cyanobacterial cells. The procedure entails precipitation, selectable depolymerization, and the detection of glucose residues. This method is suitable for both wildtype and genetically engineered strains and can facilitate the metabolic engineering of cyanobacteria.

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