SDS Protein Sample Buffer (2×)

2020 ◽  
Vol 2020 (9) ◽  
pp. pdb.rec106708
Keyword(s):  
Protein Sample

scholarly journals A High-Throughput Microchromatography Platform for Quantitative Analytical Scale Protein Sample Preparation

2011 ◽  
Vol 16 (6) ◽  
pp. 457-467 ◽  
Author(s):  
Scott Fulton ◽  
Steve Murphy ◽  
Jenn Reich ◽  
Zachary Van Den Heuvel ◽  
Robert Sakowski ◽  
...  
Keyword(s):  
Sample Preparation ◽  
High Throughput ◽  
Protein Sample ◽  
Analytical Scale ◽  
Protein Sample Preparation

2D-DIGE A Powerful Tool for Proteome Analysis

2020 ◽  
pp. 67-73
Keyword(s):  
Protein Expression ◽  
Gel Electrophoresis ◽  
Proteome Analysis ◽  
Great Sensitivity ◽  
Two Dimensional Gel Electrophoresis ◽  
2D Dige ◽  
Protein Sample ◽  
Different Types ◽  
Complex Protein ◽  
2D Gel

In the recent past, two dimensional gel electrophoresis has emerged as a powerful molecular biology tool for the comparative expression profiling of complex protein sample. It involves the separation as well as the resolution of diverse proteins sample on the basis of isoelectric points and molecular mass of protein in two dimension ways. In this way, it reflects the view of overall proteome status including differentiation in protein expression levels, post-translational modifications etc. Moreover, this allows the identification of novel biological signatures, which may give a particular identity of pathological background to cells or tissues associated with various types of cancers and neurological disorders. Therefore, by utilizing such tools, one can clearly investigate and compare the effects of particular drugs on cells of tissues and also one can analyze the effects of disease on the basis of variations in protein expression profile at broad spectrum. Recently, to get more error-less and accurate proteome profile, conventional 2-D gel electrophoresis has been enhanced with the inclusion of different types of protein labeling dyes which enables a more comparative analysis of diverse protein sample in a single 2-D gel. In this advanced technique (2-D-DIGE), protein samples are labeled with three different types of CyDyes (Cy2, Cy3, and Cy5) separately and combined and further resolved on the same gel. This will facilitate the more accurate spot matching on a single gel platform and will also minimize the experimental variations as commonly reported in the conventional 2D-gel electrophoresis. Therefore, in the present proteomic research era, 2D-DIGE has proved to be an extremely powerful tool with great sensitivity for up to 125 ng of proteins in clinical research volubility especially, neurological and cancer related disorders.

Nanomaterials in Protein Sample Preparation

2019 ◽  
Vol 49 (3) ◽  
pp. 229-264
Author(s):  
Estefanía González-García ◽  
María Luisa Marina ◽  
María Concepción García
Keyword(s):  
Sample Preparation ◽  
Protein Sample ◽  
Protein Sample Preparation

Gold nanoparticles coated with carbosilane dendrons in protein sample preparation

2019 ◽  
Vol 186 (8) ◽  
Author(s):  
Romy Vásquez-Villanueva ◽  
Cornelia E. Peña-González ◽  
Javier Sánchez-Nieves ◽  
F. Javier de la Mata ◽  
M. Luisa Marina ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Sample Preparation ◽  
Protein Sample ◽  
Protein Sample Preparation

scholarly journals Methods for Obtaining Better Diffractive Protein Crystals: From Sample Evaluation to Space Crystallization

Crystals ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 78
Author(s):  
Yoshinobu Hashizume ◽  
Koji Inaka ◽  
Naoki Furubayashi ◽  
Masayuki Kamo ◽  
Sachiko Takahashi ◽  
...  
Keyword(s):  
Crystal Growth ◽  
Quality Evaluation ◽  
Protein Crystallization ◽  
Protein Crystals ◽  
Microgravity Environment ◽  
Theoretical Understanding ◽  
Protein Sample ◽  
Space Experiments ◽  
Flash Cooling ◽  
Crystallization Conditions

In this paper, we present a summary on how to obtain protein crystals from which better diffraction images can be produced. In particular, we describe, in detail, quality evaluation of the protein sample, the crystallization conditions and methods, flash-cooling protection of the crystal, and crystallization under a microgravity environment. Our approach to protein crystallization relies on a theoretical understanding of the mechanisms of crystal growth. They are useful not only for space experiments, but also for crystallization in the laboratory.

scholarly journals Purification of viral genome-linked protein VPg from potato virus A-infected plants reveals several post-translationally modified forms of the protein

2008 ◽  
Vol 89 (6) ◽  
pp. 1509-1518 ◽  
Author(s):  
Anders Hafrén ◽  
Kristiina Mäkinen
Keyword(s):  
Potato Virus ◽  
Protein Interactions ◽  
Viral Genome ◽  
Affinity Purification ◽  
Infection Process ◽  
Dependent Manner ◽  
Affinity Tag ◽  
Post Translational Modifications ◽  
Potato Virus A ◽  
Protein Sample

In order to be able to analyse post-translational modifications and protein interactions of viral genome-linked protein VPg taking place during potato virus A (PVA) infection, an affinity tag-based purification system was developed by inserting a sequence encoding a six-histidine and haemagglutinin (HisHA) tag to the 3′ end of the VPg coding sequence within the infectious cDNA clone of PVA. The engineered virus was fully functional and the HisHA tag-encoding sequence remained stable in the PVA genome throughout the infection process. Purification under denaturing conditions resulted in a protein sample that contained multiple VPg and NIa forms carrying post-translational modifications that altered their isoelectric points. Non-modified tagged VPg (pI 8) was a minor product in the protein sample derived from total leaf proteins, but when the replication-associated membranes were used as starting material, its relative amount increased. Further characterization demonstrated that some of the PVA VPg isoforms were modified by multiple phosphorylation events. Purity of the proteins derived from the native purifications with either of the tags was evaluated. A clearly purer VPg sample was obtained by performing tandem affinity purification utilizing both tags sequentially. NIb, CI and HC-Pro co-purified in an affinity-tagged VPg-dependent manner, indicating that the system was able to isolate protein complexes operating during PVA infection.

Application of multiplexed cysteine-labeled complex protein sample for 2D electrophoretic gel alignment

PROTEOMICS ◽  
2015 ◽  
Vol 15 (11) ◽  
pp. 1777-1780 ◽  
Author(s):  
Perttu Haimi ◽  
Sidona Sikorskaite-Gudziuniene ◽  
Danas Baniulis
Keyword(s):  
Protein Sample ◽  
Complex Protein
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