SAA Antibody Monoclonal Anti-Serum Amyloid A

SAA Antibody Monoclonal Anti-Serum Amyloid A. 5 different clones are available. :_x000D_ <table width="452">_x000D_ <tbody>_x000D_ <tr>_x000D_ <td><strong>Catalog #</strong></td>_x000D_ <td>A2010002-3H7_x000D_ _x000D_ A2010002-4A9_x000D_ _x000D_ A2010002-6B3_x000D_ _x000D_ A2010002-8B6_x000D_ _x000D_ A2010002-5C10_x000D_ _x000D_ A2010002-SET</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Size</strong></td>_x000D_ <td>0.5 mg</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Other Names</strong></td>_x000D_ <td>Mab to SAA, antibody to SAA</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Host</strong></td>_x000D_ <td>Mouse</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Concentration</strong></td>_x000D_ <td>4.0 mg/mL</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Purity</strong></td>_x000D_ <td>&gt;90% (protein A column)</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Storage</strong></td>_x000D_ <td>-20°C. Avoid repeated freeze/thaw cycles.</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Supplied as</strong></td>_x000D_ <td>Liquid solution</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Buffer</strong></td>_x000D_ <td>1X Phosphate Buffer Saline, pH 7.4 + 0.05% sodium azide.</td>_x000D_ </tr>_x000D_ <tr>_x000D_ <td><strong>Keywords</strong></td>_x000D_ <td>SAA, mouse monoclonal antibody, Anti-Serum Amyloid A</td>_x000D_ </tr>_x000D_ </tbody>_x000D_ </table>_x000D_ &nbsp;_x000D_ _x000D_ <strong>References_x000D_ </strong>_x000D_ <ul>_x000D_ <li>Hepatocytes direct the formation of a pro-metastatic niche in the liver.  <span class="labs-docsum-authors full-authors">Lee JW, Stone ML, Porrett PM, Thomas SK, Komar CA, Li JH, Delman D, Graham K, Gladney WL, Hua X, Black TA, Chien AL, Majmundar KS, Thompson JC, Yee SS, O'Hara MH, Aggarwal C, Xin D, Shaked A, Gao M, Liu D, Borad MJ, Ramanathan RK, Carpenter EL, Ji A, de Beer MC, de Beer FC, Webb NR, Beatty GL.</span> <span class="labs-docsum-journal-citation full-journal-citation">Nature. 2019 Mar;567(7747):249-252.</span></li>_x000D_ <li>Serumamyloid A1 is involved in amyloid plaque aggregation and memory decline in amyloid beta abundant condition.<span class="labs-docsum-authors full-authors"> Jang S, Jang WY, Choi M, Lee J, Kwon W, Yi J, Park SJ, Yoon D, Lee S, Kim MO, Ryoo ZY.</span> <span class="labs-docsum-journal-citation full-journal-citation">Transgenic Res. 2019 Dec;28(5-6):499-508. </span></li>_x000D_ <li>Scavenger Receptor A1 Prevents Metastasis of Non-Small Cell Lung Cancer via Suppression of Macrophage SerumAmyloid A1.<span class="labs-docsum-authors full-authors"> Zhang Y, Wei Y, Jiang B, Chen L, Bai H, Zhu X, Li X, Zhang H, Yang Q, Ma J, Xu Y, Ben J, Christiani DC, Chen Q.</span> <span class="labs-docsum-journal-citation full-journal-citation">Cancer Res. 2017 Apr 1;77(7):1586-1598. </span></li>_x000D_ <li>Time-resolved fluorescent immunoassay-based combined detection of procalcitonin, C-reactive protein, heparin binding protein, and serumamyloid A1 to improve the diagnostic accuracy of early infection.<span class="labs-docsum-authors full-authors"> Niu T, Liu Y, Zhu F, Ma J, Gao J.</span> <span class="labs-docsum-journal-citation full-journal-citation">J Clin Lab Anal. 2019 Feb;33(2):e22694. </span></li>_x000D_ <li>Antifungal Activity of Mammalian Serum Amyloid A1 against Candida albicans.<span class="labs-docsum-authors full-authors"> Gong J, Wu J, Ikeh M, Tao L, Zhang Y, Bing J, Nobile CJ, Huang G.</span> <span class="labs-docsum-journal-citation full-journal-citation"><a href="https://pubmed.ncbi.nlm.nih.gov/31685470/">Antimicrob Agents Chemother.</a> 2019 Dec 20;64(1):e01975-19.</span></li>_x000D_ <li></li>_x000D_ </ul>_x000D_ <strong>Related Products</strong>_x000D_ _x000D_ https://moleculardepot.com/product/recombinant-human-serum-amyloid-a1-saa/