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The Protein Man's Blog | A Discussion of Protein Research

Using Chaotropic Extraction Buffers to Preserve the Native Charge of Protein

Posted by Protein Man on Apr 26, 2016 10:00:00 AM

chaotrapic.jpgProtein solubility is a key factor for successful 2D gel electrophoresis. Thus, the choice of protein solubilization buffers can greatly affect the results of your experiments. Proteins need to be solubilized during sample preparation and electrophoresis to break the inter- and intra-molecular interactions involved in protein aggregation (e.g. disulfide and/or hydrogen bonds, ionic and/or hydrophobic interactions, and van der Waals forces). Failure to break these interactions may result in sample loss or the formation of experimental artifacts.

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Why Is Lactate Dehydrogenase (LDH) Release A Good Measure For Cytotoxicity?

Posted by Protein Man on Mar 31, 2016 10:00:00 AM

When treated with a cytotoxic compound, living cells may face one of two fates. They could either stop growing and dividing, or die through either of two distinct processes - necrosis or apoptosis. Basically, cells undergoing necrosis (accidental cell death) swell and lose membrane integrity before shutting down and releasing their intracellular contents into the surrounding environment. This type of cell death is usually triggered by external factors such as toxic chemical or traumatic physical events.

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Should I Use A Native Or Denaturing Gel?

Posted by Protein Man on Mar 23, 2016 8:00:00 AM

Gel electrophoresis is a simple, rapid and highly sensitive tool that can be used to separate proteins based on their physical properties (e.g. molecular weight and native charge or isoelectric point) prior to downstream detection or analysis. The separation of proteins by electrophoresis can be explained by the fact that charged molecules will travel through a gel matrix when an electrical current is applied. Proteins are commonly separated in this manner using polyacrylamide gel electrophoresis (PAGE) to identify individual proteins in complex samples or to examine multiple proteins within a single sample.

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Why Today's High School Biology Classes Are Teaching Biotech

Posted by Protein Man on Mar 1, 2016 10:00:00 AM

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As you probably know, biotechnology has grown tremendously over the past decade. What you may not know, however, it is now being taught in some high school classes. This post will explore why biotech is being taught as early as high school and how this is paving the way for a new generation of biotech experts.

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Why Does Tyrosine and Tryptophan Have Effect in Protein Determination and to What Degree?

Posted by Protein Man on Feb 17, 2016 10:00:00 AM

Since accurate protein quantitation is essential to all experiments related to protein studies, different methods have been developed to measure the concentration of proteins in a given assay. Some of the more traditional methods of total protein quantitation include the measurement of UV absorbance at 280 nm (A280), Bicinchoninic acid (BCA) and Bradford assays, and other alternative methods such as Lowry and other novel assays.

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How to Safely Use Detergents during Protein Extraction

Posted by Protein Man on Feb 9, 2016 10:00:00 AM

While detergents can be used to extract, solubilize, and manipulate (disrupt or form) membrane proteins from biological membranes for subsequent biochemical and physical characterization, and are useful in controlling protein crystallization and preventing nonspecific binding in affinity purification and immunoassay procedures, they can also be one of your greatest foes in the laboratory.

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Tips for Preparing Phosphate Buffers

Posted by Protein Man on Feb 2, 2016 10:00:00 AM

When doing biological applications in the laboratory, it is essential that you have your phosphate buffers available at all times. This is of extreme importance since most biological applications are very sensitive to changes in pH, and these buffers are very effective in keeping the pH range of cellular fluids within the normal range (6.9 to 7.4).

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Coupling to Carrier Proteins: An Overview

Posted by Protein Man on Jan 27, 2016 10:00:00 AM

The use of peptides for the generation of antibodies against specific peptides has become an essential tool in proteomic research. However, while they are designed to be good epitopes by themselves, these immunogenic peptides or haptens are too small (size ranges from 1000-2000 Daltons) to elicit a strong antibody response, even when emulsified in an appropriate adjuvant.

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Selecting Protein Assays? These Are the Top Factors That Can Impact Accuracy

Posted by Protein Man on Dec 30, 2015 10:00:00 AM

The ability to accurately quantify protein concentration is the key to a successful laboratory workflow, and is often required prior to processing protein samples for isolation, separation, and analysis. To determine the total protein concentration in a sample, one of the first factors to consider is the selection of an appropriate protein assay method. However, since there are a wide variety of protein assays available, you need to take a number of factors (e.g. the accuracy required and the amount and purity of the protein available) into account to make sure that you are using the most suitable assay for your application.

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Tags: Protein Detection

Why is Trypsin the Preferred Choice for Peptide Generation?

Posted by Protein Man on Dec 8, 2015 10:30:00 AM

The serine protease trypsin (Tn) is commonly used in most proteomics experiments to digest proteins into peptides which can be analyzed by matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) or liquid chromatography-tandem mass spectrometry (LC-MS/MS).

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