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325 results for “PURIFICATION”
Expression and purification of HTT79-3144 with and without HAP40 from Sf9 Insect cells - 2019/01/28
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Expression and purification of HTT<sup>79-3144 </sup>with and without HAP40 from Sf9 Insect cells</p> <p><strong>Date completed:­ </strong>2019/01/28</p> <p><strong>Rationale: </strong>HTT lacking the unstructured region of exon1 (aa. 1-78 which are not resolved in the cryoEM model PDB ID 6EZ8) may serve as a useful control when determining exon1-dependent functionality of the HTT protein. Apo and HAP40-bound HTT<sup>79-3144 </sup>will be produced from Sf9 insect cell expression system. </p>
Optimisation of HTT-HAP40 purification using heparin affinity chromatography - 2019/01/29
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Optimisation of HTT-HAP40 purification using heparin affinity chromatography</p> <p><strong>Date completed:­ </strong>2019/01/29</p> <p><strong>Rationale: </strong>The current protocol for HTT and HTT-HAP40 purification I am using requires a long incubation of clarified cell lysate with FLAG resin. To potentially improve yields and sample quality, it would perhaps be beneficial to have a quick heparin resin purification step prior to FLAG binding which may also remove contaminating nucleic acid material. To test this hypothesis, small-scale purification of Q23 HTT-HAP40 samples in different buffer systems were conducted using heparin and FLAG affinity chromatography which showed the sample bound heparin resin – see <a href="https://zenodo.org/record/2553669">https://zenodo.org/record/2553669</a>. Now this need to be scaled up and tested more stringently. </p>
Coexpression and purification of HTT domains with HAP40 - 2018/12/03
<p><strong>Project: </strong>High resolution structural analysis of purified HTT proteins</p> <p><strong>Experiment: </strong>Coexpression and purification of HTT domains with HAP40</p> <p><strong>Date completed:­ </strong>2018/12/03</p> <p><strong>Rationale: </strong>HTT domain fragments are challenging to express and purify. However, the full-length protein sample was shown to have superior biophysical characteristics when coexpressed and purified with HAP40. As HAP40 has an extensive interaction surface with HTT, it could be possible to copurify domain fragments of HTT with HAP40, stabilizing the individual HEAT domains. </p>
Optimisation of HTT-HAP40 purification using heparin affinity chromatography - 2019/04/02
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Optimisation of HTT-HAP40 purification using heparin affinity chromatography</p> <p><strong>Date completed:­ </strong>2019/04/02</p> <p><strong>Rationale: </strong>Previous attempts to generate a much purer and homogenous HTT-HAP40 sample showed that the complex can bind heparin resin. In addition, I will incorporate helpful suggestions from scientists at the CHDI Palm Springs meeting full-length HTT research breakout group i.e. ATP wash to remove HSP proteins. The experiment will include 3 affinity chromatography steps with FLAG, heparin and NiNTA resin and finally a gel filtration step. </p>
Large-scale purification of HTT domain constructs 2019/04/01
<p><strong>Project: </strong>High resolution structural analysis of purified HTT samples</p> <p><strong>Experiment: </strong>Large-scale purification of HTT domain constructs</p> <p><strong>Date completed:­ </strong>2019/04/01</p> <p><strong>Rationale: </strong>Domain fragments of the huntingtin protein are useful reagents for examining protein-protein interaction characteristics of huntingtin and to map interaction interfaces. Stable, monodisperse and pure samples may also be amenable to high resolution structure solution by X-ray crystallography. Previously huntingtin fragments were cloned and screened for expression in small-scale (3 mL) culture experiments. Positive hits were scaled for production as detailed in the table on the next page. All previous work is described in this post:<a href="https://zenodo.org/record/2600051#.XKU89aeZPOQ">https://zenodo.org/record/2600051#.XKU89aeZPOQ</a>.</p>
Coexpression and purification of HTT and HTT-HAP40 with NEDD4L and HAP1 2019/05/02
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein and protein complex samples</p> <p><strong>Experiment: </strong>Coexpression and purification of HTT and HTT-HAP40 with NEDD4L and HAP1</p> <p><strong>Date completed:­ </strong>2019/05/02</p> <p><strong>Rationale: </strong>HAP1 and NEDD4L have been suggested as high probability interaction partners of HTT although it is unclear if they interact with HTT or HTT-HAP40. Coexpression of the constructs was conducted in baculoviral expression system (Sf9 cells) to determine if they copurify with HTT or HTT-HAP40. </p>
Purification of HTT mutant samples 2019/05/17
<p><strong>Project: </strong>Investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Purification of HTT mutant samples</p> <p><strong>Date completed:­ </strong>2019/05/27</p> <p><strong>Rationale: </strong>To assess HTT function <em>in vitro</em></p>
Large-scale stringent purification of HTT-HAP40 using heparin affinity chromatography 2019/05/12
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale stringent purification of HTT-HAP40 using heparin affinity chromatography</p> <p><strong>Date completed:­ </strong>2019/05/12</p> <p><strong>Rationale: </strong>Previous attempts to generate a much purer and homogenous HTT-HAP40 sample showed that the complex can bind heparin resin. In small-scale experiment, I also incorporated helpful suggestions from scientists at the CHDI Palm Springs meeting full-length HTT research breakout group i.e. ATP wash to remove HSP proteins. The experiment included 3 affinity chromatography steps with FLAG, heparin and NiNTA resin and finally a gel filtration step and yielded a highly pure HTT-HAP40 sample: <a href="https://zenodo.org/record/2628064">https://zenodo.org/record/2628064</a>. </p>
Large-scale stringent purification of Q23 HTT and HTT-HAP40 using heparin affinity chromatography 2019/05/22
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>Large-scale stringent purification of Q23 HTT and HTT-HAP40 using heparin affinity chromatography</p> <p><strong>Date completed:­ </strong>2019/05/22</p> <p><strong>Rationale: </strong>Previous attempts to generate a much purer and homogenous HTT-HAP40 sample showed that the complex can bind heparin resin. In small-scale experiment, I also incorporated helpful suggestions from scientists at the CHDI Palm Springs meeting full-length HTT research breakout group i.e. ATP wash to remove HSP proteins. The experiment included 3 affinity chromatography steps with FLAG, heparin and NiNTA resin and finally a gel filtration step and yielded a highly pure HTT-HAP40 sample: https://zenodo.org/record/3234174.I now want to try this purification with apo HTT. </p>
RAB1B Expression and Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, RAB1B was flagged. This purification aims to provide a RAB1B sample for future experiments to confirm the possible interaction between these proteins. </p>
RAB1A Expression and Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, RAB1A was flagged. This purification aims to provide a sample of RAB1A for future experiments to confirm the possible interaction between these proteins.</p>
MECP2 Expression and Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, MECP2 was flagged. This purification aims to provide a MECP2 sample for future experiments to confirm the possible interaction between these proteins.</p>
PACN1 Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, PACN1 was flagged. This purification aims to provide a PACN1 sample for future experiments to confirm the possible interaction between these proteins.</p>
SH3G3 Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, SH3G3 was flagged. This purification aims to provide a SH3G3 sample for future experiments to confirm the possible interaction between these proteins.</p>
HAP1 Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, HAP1 was flagged. This purification aims to provide a HAP1 sample for future experiments to confirm the possible interaction between these proteins. </p>
UBE2K Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, UBE2K was flagged. This purification aims to provide a UBE2K sample for future experiments to confirm the possible interaction between these proteins. </p>
NEDD4L Purification
<p>As a result of a BioID experiment done to identify possible interaction partners of Huntingtin, NEDD4L was flagged. This purification aims to provide a NEDD4L sample for future experiments to confirm the possible interaction between these proteins. </p>
Purification of the HTT C-HEAT domain (2088-3144)
<p>The purification of HTT fragments is a useful approach to learn more about the function of huntingtin in the cell. By obtaining soluble and monomeric samples of HTT domains namely the HTT 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>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 successful purification of a monomeric and mono disperse sample of the HTT C-HEAT domain. The results here presented are a follow up of those experiments and aim to further characterize the HTT C-HEAT domain as well as explore strategies to improve buffer conditions for crystallization purposes.</p>
PIAS1 Production and 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, PIAS1 was flagged. This purification aims to provide a PIAS1 sample for future experiments to confirm the possible interaction between these proteins.</p>
P97 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, P97 (uniprotID: P55072) was flagged as a putative interaction partner. This purification aims to provide a P97 sample for future experiments to confirm the possibility of an interaction between these proteins.</p>
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