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325 results for “PURIFICATION”
HIP1 Purification
<p>As a result of a <a href="https://zenodo.org/record/3234159#.XRyqiuhKjct">BioID experiment</a> and literate analysis done to identify possible interaction partners of Huntingtin, HIP1 (uniprotID: O00291) was flagged as a putative interaction partner. This purification aims to provide a HIP1 sample for future experiments to confirm the possibility of an interaction between these proteins.</p>
OPTN Purification
<p>As a result of a <a href="https://zenodo.org/record/3234159#.XRyqiuhKjct">BioID experiment</a> done to identify possible interaction partners of Huntingtin, OPTN was flagged. This purification aims to provide an OPTN sample for future experiments to confirm the possible interaction between these proteins.</p>
SQSTM1 Purification
<p>As a result of a <a href="https://zenodo.org/record/3234159#.XRyqiuhKjct">BioID experiment</a> and literate analysis done to identify possible interaction partners of Huntingtin, SQSTM1(uniprotID: Q13501) was flagged as a putative interaction partner. This purification aims to provide a SQSTM1 sample for future experiments to confirm the possibility of an interaction between these proteins.</p>
PIAS1 (full length) Purification
<p>Huntington’s Disease (HD) is a hereditary neurodegenerative disease. The cause of this disease is a CAG repeat extension in the HTT Gene. This extension is translated into an elongation of exon 1 in Huntingtin protein. Although we know the cause, the mechanism of this disease still eludes us. A part of the difficulty is our lack of understanding of the role of normal HTT in our cells. We at the SGC have set out to explore the HTT interactome to further our understanding of the role of HTT. This will give us a better basis for further study of mutant Huntingtin. Our first step on this journey was to conduct a literature review alongside a BioID experiment to come up with a list of putative huntingtin interaction partners. One of the hits on the list was PIAS1. This means that we must obtain a pure sample of PIAS1 for use in future experiments to further validate the claim that these proteins interact. Previously, I purified a shorter construct of PIAS1 in E. coli : 10.5281/zenodo.3367282. At the SGC we have access to many different constructs of the same protein. The previously purified product was only a portion of the full protein. For physiological relevance, it is important to test full length proteins so we decided to order another purification of PIAS1, and this time try to purify the whole protein. <br> </p>
GFP Production and Purification
<p><strong>Huntington’s Disease (HD) is a hereditary neurodegenerative disease. The cause of this disease is a CAG repeat extension in the HTT Gene. This extension is then translated into an elongation of exon 1 which is primarily composed of a disordered PolyQ repeat. Although the cause is known, the mechanism by which this extension affects the function of Huntingtin (HTT), the protein produced by the HTT Gene, has yet to be understood. A part of this difficulty is our lack of understanding of the role of normal HTT in our cells. During the production of pure HTT sample, we began to notice an accumulation of nucleic acid material. To test the identity of this material, we sent it to one of our collaborators who told us it was RNA. Now, we are interested in preforming CLIP-seq to identify the specific sequence bound to HTT. Standard expression methods have been found to have minimal success due to the sheer size of HTT so other methods are being explored. One of which, is inserting formed protein into the neuronal cells via electroporation as described by Lambert, H. et. al. in Electroporation - mediated uptake of proteins into mammalian cells . By importing tagged protein into neuronal cells, we hope to capture a more readable RNA sequence, giving us a clue about its cellular function. To get the protein into the cell, we are planning to use electroporation. This process can be quite variable dependent upon the equipment used and the cells used, etc. we are using GFP to optimize conditions as it is quite easy to image in cells. In order to continue with this, a concentrated GFP sample must be made. </strong></p>
Growth and Purification of Biotinylated USP5 Constructs & Testing ZnF-UBD Ligands in a Displacement Assay
<p>Expression and purification of biotinylated full length (FL) USP5<sup>1-835</sup> and biotinylated zinc finger ubiquitin-binding domain (ZnF-UBD) USP5<sup>171-290 </sup>constructs for the development of a displacement assay. </p>
Purification of HTT N-HEAT_81-1643
<p>The purification of huntingtin (HTT) fragments is a useful approach to learn more about the function of HTT in the cell. By obtaining soluble and monomeric samples of HTT domains namely the C-HEAT, N-HEAT and bridge domains, specific protein-protein interactions can be studied. Furthermore, domains of HTT in soluble monomeric form could enable crystallization studies. </p> <p>The first expression and purification of these fragments can be found on these posts <a href="https://zenodo.org/record/2600051#.XKU89aeZPOQ">https://zenodo.org/record/2600051#.XKU89aeZPOQ</a> and <a href="https://zenodo.org/record/2628060#.XULMtnspDb0">https://zenodo.org/record/2628060#.XULMtnspDb0</a> (performed by Dr. Rachel Harding). The latest post shows the purification of construct the HTT N-HEAT_81-1643 domain which elutes from Superdex 200 10/300 GL column in the void volume. The results here presented are a follow up of that purification.</p>
Expression test and purification of SETDB1 catalytic domain constructs' for structural studies by X-ray crystallography.
<p><strong>Experiment: </strong>Expression test and purification of SETDB1 catalytic domain constructs’ for structural studies by X-ray crystallography.</p> <p><strong>Aim:</strong> In the present section of this study, we focused on the development of efficient bacterial expression systems to produce large amounts of soluble SETDB1 catalytic domain for structural studies. This report involves a summary of expression test results of different fragments of SETDB1 and purification of various fusion proteins.</p>
Purification of Q23 and Q54 HTT and HTT-HAP40 from Sf9 2019/10/07
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Purification of Q23 and Q54 HTT and HTT-HAP40 from Sf9 </p> <p><strong>Date completed:­ </strong>2019/10/07</p> <p><strong>Rationale: </strong>Purification of HTT and HTT-HAP40 Q23 and Q54 for different biophysical and functional analyses</p>
Purification of HTT Q23 and Q54 from EXPI293F for mass spectrometry analysis 2019/09/30
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Purification of Q23 and Q54 HTT from EXPI293F</p> <p><strong>Date completed:­ </strong>2019/09/30</p> <p><strong>Rationale: </strong>Purify HTT Q23 and Q54 for mass spectrometry analysis</p>
Large-scale purification of Q23 HTT from Sf9 2019/09/30
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale purification of Q23 HTT from Sf9 </p> <p><strong>Date completed:­ </strong>2019/09/30</p> <p><strong>Rationale: </strong>HTT samples are to be purified from different systems for subsequent biophysical and structural studies. </p>
Large-scale purification of Q23 HTT-HAP40 from Sf9 expression system with contaminating nucleic acid material 2019/09/16
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale purification of Q23 HTT-HAP40 from Sf9 expression system with contaminating nucleic acid material</p> <p><strong>Date completed:­ </strong>2019/09/16</p> <p><strong>Rationale:</strong> To purify HTT-HAP40 + Sf9 derived nucleic acid material for cryoEM analysis</p>
Large-scale purification of Q23 and Q54 HTT-HAP40 from Sf9 expression system in PBS 2019/09/16
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale purification of Q23 and Q54 HTT-HAP40 from Sf9 expression system in PBS.</p> <p><strong>Date completed:­ </strong>2019/09/16</p> <p><strong>Rationale: </strong>To purify HTT-HAP40 Q23 and Q54 in PBS to see if this reduces nucleic acid contamination.</p>
DEVELOPMENT OF AN INNOVATIVE PROCESS INVOLVING THE USE IONIC LIQUIDS FOR THE RECOVERY AND PURIFICATION OF RARE EARTH FROM PERMANENT MAGNETS AND NiMH BATTERIES
<p>Experimental data</p>
Expression and Purification of DNA-binding domain of T-box Transcription Factor TBXTA-c021
<p>A detailed protocol for the expression and purification of G177D variant of TBXT DNA-binding domain.</p>
Expression and Purification of Full-Length T-box Transcription Factor TBXTA-c027
<p>A detailed protocol for the expression and purification of G177D variant of biotinylated, full-length TBXT</p>
Files associated with Purification of Human beta and gamma Actin from Budding Yeast
<p>Original imaging files, gels, and analyzed data associated with the paper</p>
Recombinant Expression and Purification of ABHD2 from E. coli
<p>α/β Hydrolase domain-containing protein 2 (ABHD2), is a member of the metabolic serine hydrolases superfamily & a progesterone membrane receptor. In sperm, it supports the activation of CatSper which leads to sperm hypermotility. ABHD2 is 425 aa and has a N-terminal transmembrane domain followed by an extracellular facing domain. Here we report the recombinant expression and purification of ABHD2 amino acids 33-435 from <em>E. coli</em>. To the best of our knowledge, we are the first to have recombinantly purified active ABHD2.</p>
Tandem-affinity purification of OOPS-1 and SPE-11 and identification of phosphorylation sites on OOPS-1 and SPE-11
Open the record for dataset details and reuse information.
RBBP4__1-425_NHis_Expression and Purification Protocol
<p>RBBP4__1-425_NHis_Expression and Purification Protocol</p>
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