Silk Fibroin (Bombyx Mori Silkworm)

<strong>Silk Fibroin</strong>_x000D_ <table width="452">_x000D_ <tbody>_x000D_ <tr>_x000D_ <td><strong>Size</strong></td>_x000D_ <td>50 mg</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Other Names</strong></td>_x000D_ <td>Silkworm protein</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Concentration</strong></td>_x000D_ <td>25 mg/mL</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Molecular Weight</strong></td>_x000D_ <td>100 kDa (average)</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Storage</strong></td>_x000D_ <td>2-8°C (short term). -20°C (long term). Avoid repeated freeze-thaw.</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Source</strong></td>_x000D_ <td><em>Bombyx mori </em>silkworm</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>pI</strong></td>_x000D_ <td>2.5</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Keywords</strong></td>_x000D_ <td>Fibroin, Silkworm</td>_x000D_ </tr>_x000D_ </tbody>_x000D_ </table>_x000D_ &nbsp;_x000D_ _x000D_ <strong>References</strong>_x000D_ <ul>_x000D_ <li>Advancing the frontiers of silk fibroin protein-based materials for futuristic electronics and clinical wound-healing (Invited review). <span class="labs-docsum-authors full-authors">Koh LD, Yeo J, Lee YY, Ong Q, Han M, Tee BC.</span> <span class="labs-docsum-journal-citation full-journal-citation">Mater Sci Eng C Mater Biol Appl. 2018 May 1;86:151-172.</span></li>_x000D_ <li>Rhodamine binds to silkfibroin and inhibits its self-aggregation.<span class="labs-docsum-authors full-authors"> Ragona L, Gasymov O, Guliyeva AJ, Aslanov RB, Zanzoni S, Botta C, Molinari H.</span> <span class="labs-docsum-journal-citation full-journal-citation">Biochim Biophys Acta Proteins Proteom. 2018 May-Jun;1866(5-6):661-667.</span></li>_x000D_ <li>Dissolution behavior of silkfibroin in a low concentration CaCl(2)-methanol solvent: From morphology to nanostructure.<span class="labs-docsum-authors full-authors"> Shen T, Wang T, Cheng G, Huang L, Chen L, Wu D.</span> <span class="labs-docsum-journal-citation full-journal-citation">Int J Biol Macromol. 2018 Jul 1;113:458-463.</span></li>_x000D_ <li>SilkFibroin Films Facilitate Single-Step Targeted Expression of Optogenetic Proteins.<span class="labs-docsum-authors full-authors"> Jackman SL, Chen CH, Chettih SN, Neufeld SQ, Drew IR, Agba CK, Flaquer I, Stefano AN, Kennedy TJ, Belinsky JE, Roberston K, Beron CC, Sabatini BL, Harvey CD, Regehr WG.</span> <span class="labs-docsum-journal-citation full-journal-citation">Cell Rep. 2018 Mar 20;22(12):3351-3361.</span></li>_x000D_ <li>Silkfibroin/chitosan thin film promotes osteogenic and adipogenic differentiation of rat bone marrow-derived mesenchymal stem cells.<span class="labs-docsum-authors full-authors"> Li DW, He J, He FL, Liu YL, Liu YY, Ye YJ, Deng X, Yin DC.</span> <span class="labs-docsum-journal-citation full-journal-citation">J Biomater Appl. 2018 Apr;32(9):1164-1173. </span></li>_x000D_ <li>Silkfibroin preserves beta cell function under inflammatory stress while stimulating islet cell surface GLUT2 expression.<span class="labs-docsum-authors full-authors"> Ashari N, Pang HW, Simon T, Xiong Y, Coburn JM, Bromberg JS, Kaplan DL, McLenithan J, Fontaine MJ.</span> <span class="labs-docsum-journal-citation full-journal-citation">Cell Immunol. 2018 Jul;329:10-16.</span></li>_x000D_ <li>Modulation of aggregation of silkfibroin by synergistic effect of the complex of curcumin and β-cyclodextrin.<span class="labs-docsum-authors full-authors"> Dubey P, Chowdhury PK, Ghosh S.</span> <span class="labs-docsum-journal-citation full-journal-citation">Biochim Biophys Acta Proteins Proteom. 2019 Apr;1867(4):416-425. </span></li>_x000D_ <li>Sericin Promotes Fibroin Silk I Stabilization Across a Phase-Separation.<span class="labs-docsum-authors full-authors"> Kwak HW, Ju JE, Shin M, Holland C, Lee KH.</span> <span class="labs-docsum-journal-citation full-journal-citation"><a href="https://pubmed.ncbi.nlm.nih.gov/28603980/">Biomacromolecules</a>. 2017 Aug 14;18(8):2343-2349. </span></li>_x000D_ </ul>