{"id":123573,"date":"2025-12-25T22:20:27","date_gmt":"2025-12-25T22:20:27","guid":{"rendered":"https:\/\/advbiomart.sytech.site\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/"},"modified":"2025-12-25T22:20:29","modified_gmt":"2025-12-25T22:20:29","slug":"recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319","status":"publish","type":"product","link":"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/","title":{"rendered":"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated"},"content":{"rendered":"","protected":false},"excerpt":{"rendered":"<p>Activating transcription factor 7-interacting protein 1 (ATF7IP) is a multifunctional protein involved in various cellular processes. It has been shown to interact with methylated DNA-binding domain protein 1 (MBD1) and MBD1-containing chromatin-associated factor 1 (MCAF1), also known as ATFaassociated modulator (AM) [1]. ATF7IP is implicated in the maintenance of X chromosome inactivation (XCI) through its repressive context, where it mediates MBD1-dependent transcriptional silencing by recruiting and catalytically activating the histone H3K9 methyltransferase SETDB1 [2]. Furthermore, ATF7IP contains at least two functional binding surfaces for other proteins, such as SETDB1 and MBD1, and plays a role in efficient transcriptional silencing mediated by the SETDB1 complex [3][4]. It has also been identified as a transcriptional cofactor involved in histone gene expression and cellular senescence [5]. ATF7IP is recognized as a SETDB1-interacting protein and is essential for heterochromatin formation by the HUSH complex [6]. Additionally, ATF7IP has been reported to inhibit Il2 expression, regulating Th17 responses, and is an essential cofactor in SETDB1 enzymatic activity and nuclear localization [7]. Moreover, ATF7IP is involved in the regulation of SETDB1 nuclear localization and its enzymatic activity, as well as in increasing the levels of its ubiquitinated and more enzymatically active forms [8][9]. The protein also undergoes tri-methylation by G9a\/GLP, recruiting the chromodomain protein MPP8, suggesting its involvement in gene regulation [10]. Interestingly, ATF7IP&#8217;s methylation partially contributes to the function of the HUSH complex, as preventing K16 methylation led to a delay in HUSH complex silencing of a virally introduced transgene [11].<br \/>\nReferences:[1] L. Liu, K. Ishihara, T. Ichimura, N. Fujita, S. Hino, S. Tomitaet al., &#8220;Mcaf1\/am is involved in sp1-mediated maintenance of cancer-associated telomerase activity&#8221;, Journal of Biological Chemistry, vol. 284, no. 8, p. 5165-5174, 2009. https:\/\/doi.org\/10.1074\/jbc.m807098200[2] A. Minkovsky, A. Sahakyan, E. Rankin-Gee, G. Bonora, S. Patel, &#038; K. Plath, &#8220;The mbd1-atf7ip-setdb1 pathway contributes to the maintenance of x chromosome inactivation&#8221;, Epigenetics &#038; Chromatin, vol. 7, no. 1, 2014. https:\/\/doi.org\/10.1186\/1756-8935-7-12[3] T. Tsusaka, K. Fukuda, C. Shimura, M. Kato, &#038; Y. Shinkai, &#8220;The fibronectin type-iii (fniii) domain of atf7ip contributes to efficient transcriptional silencing mediated by the setdb1 complex&#8221;, Epigenetics &#038; Chromatin, vol. 13, no. 1, 2020. https:\/\/doi.org\/10.1186\/s13072-020-00374-4[4] Y. Li, B. Sun, L. Xu, L. Chen, &#038; W. Ou, &#8220;The updating of biological functions of methyltransferase setdb1 and its relevance in lung cancer and mesothelioma&#8221;, International Journal of Molecular Sciences, vol. 22, no. 14, p. 7416, 2021. https:\/\/doi.org\/10.3390\/ijms22147416[5] N. Sasai, N. Saitoh, H. Saitoh, &#038; M. Nakao, &#8220;The transcriptional cofactor mcaf1\/atf7ip is involved in histone gene expression and cellular senescence&#8221;, Plos One, vol. 8, no. 7, p. e68478, 2013. https:\/\/doi.org\/10.1371\/journal.pone.0068478[6] R. Timms, I. Tchasovnikarova, R. Antrobus, G. Dougan, &#038; P. Lehner, &#8220;Atf7ip-mediated stabilization of the histone methyltransferase setdb1 is essential for heterochromatin formation by the hush complex&#8221;, Cell Reports, vol. 17, no. 3, p. 653-659, 2016. https:\/\/doi.org\/10.1016\/j.celrep.2016.09.050[7] J. Sin, C. Zuckerman, J. Cortez, W. Eckalbar, D. Erle, M. Andersonet al., &#8220;The epigenetic regulator atf7ip inhibits il2 expression, regulating th17 responses&#8221;, The Journal of Experimental Medicine, vol. 216, no. 9, p. 2024-2037, 2019. https:\/\/doi.org\/10.1084\/jem.20182316[8] T. Tsusaka, C. Shimura, &#038; Y. Shinkai, &#8220;Atf7ip regulates setdb1 nuclear localization and increases its ubiquitination&#8221;, Embo Reports, vol. 20, no. 12, 2019. https:\/\/doi.org\/10.15252\/embr.201948297[9] Y. Shinkai, T. Tsusaka, K. Fukuda, C. Shimura, &#038; M. Kato, &#8220;The fibronectin type-iii (fniii) domain of atf7ip contributes to efficient transcriptional silencing mediated by the setdb1 complex&amp;nbsp;&#8221;,, 2020. https:\/\/doi.org\/10.21203\/rs.3.rs-44959\/v2[10] T. Tsusaka, M. Kikuchi, T. Shimazu, T. Suzuki, Y. Sohtome, M. Akakabeet al., &#8220;Tri-methylation of atf7ip by g9a\/glp recruits the chromodomain protein mpp8&#8221;, Epigenetics &#038; Chromatin, vol. 11, no. 1, 2018. https:\/\/doi.org\/10.1186\/s13072-018-0231-z[11] E. Cornett, L. Ferry, P. Defossez, &#038; S. Rothbart, &#8220;Lysine methylation regulators moonlighting outside the epigenome&#8221;, Molecular Cell, vol. 75, no. 6, p. 1092-1101, 2019. https:\/\/doi.org\/10.1016\/j.molcel.2019.08.026<\/p>\n","protected":false},"featured_media":0,"comment_status":"open","ping_status":"closed","template":"","meta":{"_acf_changed":false},"product_brand":[],"product_cat":[168834,18],"product_tag":[93726],"class_list":["post-123573","product","type-product","status-publish","product_cat-proteins","product_cat-recombinant-proteins","product_tag-atf7ip","first","instock","shipping-taxable","product-type-simple"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v27.0 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated - AbTrivia<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/\" \/>\n<meta property=\"og:locale\" content=\"es_ES\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated - AbTrivia\" \/>\n<meta property=\"og:description\" content=\"Activating transcription factor 7-interacting protein 1 (ATF7IP) is a multifunctional protein involved in various cellular processes. It has been shown to interact with methylated DNA-binding domain protein 1 (MBD1) and MBD1-containing chromatin-associated factor 1 (MCAF1), also known as ATFaassociated modulator (AM) [1]. ATF7IP is implicated in the maintenance of X chromosome inactivation (XCI) through its repressive context, where it mediates MBD1-dependent transcriptional silencing by recruiting and catalytically activating the histone H3K9 methyltransferase SETDB1 [2]. Furthermore, ATF7IP contains at least two functional binding surfaces for other proteins, such as SETDB1 and MBD1, and plays a role in efficient transcriptional silencing mediated by the SETDB1 complex [3][4]. It has also been identified as a transcriptional cofactor involved in histone gene expression and cellular senescence [5]. ATF7IP is recognized as a SETDB1-interacting protein and is essential for heterochromatin formation by the HUSH complex [6]. Additionally, ATF7IP has been reported to inhibit Il2 expression, regulating Th17 responses, and is an essential cofactor in SETDB1 enzymatic activity and nuclear localization [7]. Moreover, ATF7IP is involved in the regulation of SETDB1 nuclear localization and its enzymatic activity, as well as in increasing the levels of its ubiquitinated and more enzymatically active forms [8][9]. The protein also undergoes tri-methylation by G9a\/GLP, recruiting the chromodomain protein MPP8, suggesting its involvement in gene regulation [10]. Interestingly, ATF7IP&#039;s methylation partially contributes to the function of the HUSH complex, as preventing K16 methylation led to a delay in HUSH complex silencing of a virally introduced transgene [11]. References:[1] L. Liu, K. Ishihara, T. Ichimura, N. Fujita, S. Hino, S. Tomitaet al., &quot;Mcaf1\/am is involved in sp1-mediated maintenance of cancer-associated telomerase activity&quot;, Journal of Biological Chemistry, vol. 284, no. 8, p. 5165-5174, 2009. https:\/\/doi.org\/10.1074\/jbc.m807098200[2] A. Minkovsky, A. Sahakyan, E. Rankin-Gee, G. Bonora, S. Patel, &amp; K. Plath, &quot;The mbd1-atf7ip-setdb1 pathway contributes to the maintenance of x chromosome inactivation&quot;, Epigenetics &amp; Chromatin, vol. 7, no. 1, 2014. https:\/\/doi.org\/10.1186\/1756-8935-7-12[3] T. Tsusaka, K. Fukuda, C. Shimura, M. Kato, &amp; Y. Shinkai, &quot;The fibronectin type-iii (fniii) domain of atf7ip contributes to efficient transcriptional silencing mediated by the setdb1 complex&quot;, Epigenetics &amp; Chromatin, vol. 13, no. 1, 2020. https:\/\/doi.org\/10.1186\/s13072-020-00374-4[4] Y. Li, B. Sun, L. Xu, L. Chen, &amp; W. Ou, &quot;The updating of biological functions of methyltransferase setdb1 and its relevance in lung cancer and mesothelioma&quot;, International Journal of Molecular Sciences, vol. 22, no. 14, p. 7416, 2021. https:\/\/doi.org\/10.3390\/ijms22147416[5] N. Sasai, N. Saitoh, H. Saitoh, &amp; M. Nakao, &quot;The transcriptional cofactor mcaf1\/atf7ip is involved in histone gene expression and cellular senescence&quot;, Plos One, vol. 8, no. 7, p. e68478, 2013. https:\/\/doi.org\/10.1371\/journal.pone.0068478[6] R. Timms, I. Tchasovnikarova, R. Antrobus, G. Dougan, &amp; P. Lehner, &quot;Atf7ip-mediated stabilization of the histone methyltransferase setdb1 is essential for heterochromatin formation by the hush complex&quot;, Cell Reports, vol. 17, no. 3, p. 653-659, 2016. https:\/\/doi.org\/10.1016\/j.celrep.2016.09.050[7] J. Sin, C. Zuckerman, J. Cortez, W. Eckalbar, D. Erle, M. Andersonet al., &quot;The epigenetic regulator atf7ip inhibits il2 expression, regulating th17 responses&quot;, The Journal of Experimental Medicine, vol. 216, no. 9, p. 2024-2037, 2019. https:\/\/doi.org\/10.1084\/jem.20182316[8] T. Tsusaka, C. Shimura, &amp; Y. Shinkai, &quot;Atf7ip regulates setdb1 nuclear localization and increases its ubiquitination&quot;, Embo Reports, vol. 20, no. 12, 2019. https:\/\/doi.org\/10.15252\/embr.201948297[9] Y. Shinkai, T. Tsusaka, K. Fukuda, C. Shimura, &amp; M. Kato, &quot;The fibronectin type-iii (fniii) domain of atf7ip contributes to efficient transcriptional silencing mediated by the setdb1 complex&amp;nbsp;&quot;,, 2020. https:\/\/doi.org\/10.21203\/rs.3.rs-44959\/v2[10] T. Tsusaka, M. Kikuchi, T. Shimazu, T. Suzuki, Y. Sohtome, M. Akakabeet al., &quot;Tri-methylation of atf7ip by g9a\/glp recruits the chromodomain protein mpp8&quot;, Epigenetics &amp; Chromatin, vol. 11, no. 1, 2018. https:\/\/doi.org\/10.1186\/s13072-018-0231-z[11] E. Cornett, L. Ferry, P. Defossez, &amp; S. Rothbart, &quot;Lysine methylation regulators moonlighting outside the epigenome&quot;, Molecular Cell, vol. 75, no. 6, p. 1092-1101, 2019. https:\/\/doi.org\/10.1016\/j.molcel.2019.08.026\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/\" \/>\n<meta property=\"og:site_name\" content=\"AbTrivia\" \/>\n<meta property=\"article:modified_time\" content=\"2025-12-25T22:20:29+00:00\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"WebPage\",\"@id\":\"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/\",\"url\":\"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/\",\"name\":\"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated - AbTrivia\",\"isPartOf\":{\"@id\":\"https:\/\/abtriva.com\/cn\/#website\"},\"datePublished\":\"2025-12-25T22:20:27+00:00\",\"dateModified\":\"2025-12-25T22:20:29+00:00\",\"breadcrumb\":{\"@id\":\"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/#breadcrumb\"},\"inLanguage\":\"es_ES\",\"potentialAction\":[{\"@type\":\"ReadAction\",\"target\":[\"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/\"]}]},{\"@type\":\"BreadcrumbList\",\"@id\":\"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/#breadcrumb\",\"itemListElement\":[{\"@type\":\"ListItem\",\"position\":1,\"name\":\"Home\",\"item\":\"https:\/\/www.abtriva.com\/es\/\"},{\"@type\":\"ListItem\",\"position\":2,\"name\":\"Products\",\"item\":\"https:\/\/www.abtriva.com\/es\/shop\/\"},{\"@type\":\"ListItem\",\"position\":3,\"name\":\"Proteins\",\"item\":\"https:\/\/www.abtriva.com\/es\/category\/proteins\/\"},{\"@type\":\"ListItem\",\"position\":4,\"name\":\"Recombinant Proteins\",\"item\":\"https:\/\/www.abtriva.com\/es\/category\/proteins\/recombinant-proteins\/\"},{\"@type\":\"ListItem\",\"position\":5,\"name\":\"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated\"}]},{\"@type\":\"WebSite\",\"@id\":\"https:\/\/abtriva.com\/cn\/#website\",\"url\":\"https:\/\/abtriva.com\/cn\/\",\"name\":\"AbTrivia\",\"description\":\"\",\"potentialAction\":[{\"@type\":\"SearchAction\",\"target\":{\"@type\":\"EntryPoint\",\"urlTemplate\":\"https:\/\/abtriva.com\/cn\/?s={search_term_string}\"},\"query-input\":{\"@type\":\"PropertyValueSpecification\",\"valueRequired\":true,\"valueName\":\"search_term_string\"}}],\"inLanguage\":\"es_ES\"}]}<\/script>\n<!-- \/ Yoast SEO plugin. -->","yoast_head_json":{"title":"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated - AbTrivia","robots":{"index":"index","follow":"follow","max-snippet":"max-snippet:-1","max-image-preview":"max-image-preview:large","max-video-preview":"max-video-preview:-1"},"canonical":"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/","og_locale":"es_ES","og_type":"article","og_title":"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated - AbTrivia","og_description":"Activating transcription factor 7-interacting protein 1 (ATF7IP) is a multifunctional protein involved in various cellular processes. It has been shown to interact with methylated DNA-binding domain protein 1 (MBD1) and MBD1-containing chromatin-associated factor 1 (MCAF1), also known as ATFaassociated modulator (AM) [1]. ATF7IP is implicated in the maintenance of X chromosome inactivation (XCI) through its repressive context, where it mediates MBD1-dependent transcriptional silencing by recruiting and catalytically activating the histone H3K9 methyltransferase SETDB1 [2]. Furthermore, ATF7IP contains at least two functional binding surfaces for other proteins, such as SETDB1 and MBD1, and plays a role in efficient transcriptional silencing mediated by the SETDB1 complex [3][4]. It has also been identified as a transcriptional cofactor involved in histone gene expression and cellular senescence [5]. ATF7IP is recognized as a SETDB1-interacting protein and is essential for heterochromatin formation by the HUSH complex [6]. Additionally, ATF7IP has been reported to inhibit Il2 expression, regulating Th17 responses, and is an essential cofactor in SETDB1 enzymatic activity and nuclear localization [7]. Moreover, ATF7IP is involved in the regulation of SETDB1 nuclear localization and its enzymatic activity, as well as in increasing the levels of its ubiquitinated and more enzymatically active forms [8][9]. The protein also undergoes tri-methylation by G9a\/GLP, recruiting the chromodomain protein MPP8, suggesting its involvement in gene regulation [10]. Interestingly, ATF7IP's methylation partially contributes to the function of the HUSH complex, as preventing K16 methylation led to a delay in HUSH complex silencing of a virally introduced transgene [11]. References:[1] L. Liu, K. Ishihara, T. Ichimura, N. Fujita, S. Hino, S. Tomitaet al., \"Mcaf1\/am is involved in sp1-mediated maintenance of cancer-associated telomerase activity\", Journal of Biological Chemistry, vol. 284, no. 8, p. 5165-5174, 2009. https:\/\/doi.org\/10.1074\/jbc.m807098200[2] A. Minkovsky, A. Sahakyan, E. Rankin-Gee, G. Bonora, S. Patel, & K. Plath, \"The mbd1-atf7ip-setdb1 pathway contributes to the maintenance of x chromosome inactivation\", Epigenetics & Chromatin, vol. 7, no. 1, 2014. https:\/\/doi.org\/10.1186\/1756-8935-7-12[3] T. Tsusaka, K. Fukuda, C. Shimura, M. Kato, & Y. Shinkai, \"The fibronectin type-iii (fniii) domain of atf7ip contributes to efficient transcriptional silencing mediated by the setdb1 complex\", Epigenetics & Chromatin, vol. 13, no. 1, 2020. https:\/\/doi.org\/10.1186\/s13072-020-00374-4[4] Y. Li, B. Sun, L. Xu, L. Chen, & W. Ou, \"The updating of biological functions of methyltransferase setdb1 and its relevance in lung cancer and mesothelioma\", International Journal of Molecular Sciences, vol. 22, no. 14, p. 7416, 2021. https:\/\/doi.org\/10.3390\/ijms22147416[5] N. Sasai, N. Saitoh, H. Saitoh, & M. Nakao, \"The transcriptional cofactor mcaf1\/atf7ip is involved in histone gene expression and cellular senescence\", Plos One, vol. 8, no. 7, p. e68478, 2013. https:\/\/doi.org\/10.1371\/journal.pone.0068478[6] R. Timms, I. Tchasovnikarova, R. Antrobus, G. Dougan, & P. Lehner, \"Atf7ip-mediated stabilization of the histone methyltransferase setdb1 is essential for heterochromatin formation by the hush complex\", Cell Reports, vol. 17, no. 3, p. 653-659, 2016. https:\/\/doi.org\/10.1016\/j.celrep.2016.09.050[7] J. Sin, C. Zuckerman, J. Cortez, W. Eckalbar, D. Erle, M. Andersonet al., \"The epigenetic regulator atf7ip inhibits il2 expression, regulating th17 responses\", The Journal of Experimental Medicine, vol. 216, no. 9, p. 2024-2037, 2019. https:\/\/doi.org\/10.1084\/jem.20182316[8] T. Tsusaka, C. Shimura, & Y. Shinkai, \"Atf7ip regulates setdb1 nuclear localization and increases its ubiquitination\", Embo Reports, vol. 20, no. 12, 2019. https:\/\/doi.org\/10.15252\/embr.201948297[9] Y. Shinkai, T. Tsusaka, K. Fukuda, C. Shimura, & M. Kato, \"The fibronectin type-iii (fniii) domain of atf7ip contributes to efficient transcriptional silencing mediated by the setdb1 complex&amp;nbsp;\",, 2020. https:\/\/doi.org\/10.21203\/rs.3.rs-44959\/v2[10] T. Tsusaka, M. Kikuchi, T. Shimazu, T. Suzuki, Y. Sohtome, M. Akakabeet al., \"Tri-methylation of atf7ip by g9a\/glp recruits the chromodomain protein mpp8\", Epigenetics & Chromatin, vol. 11, no. 1, 2018. https:\/\/doi.org\/10.1186\/s13072-018-0231-z[11] E. Cornett, L. Ferry, P. Defossez, & S. Rothbart, \"Lysine methylation regulators moonlighting outside the epigenome\", Molecular Cell, vol. 75, no. 6, p. 1092-1101, 2019. https:\/\/doi.org\/10.1016\/j.molcel.2019.08.026","og_url":"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/","og_site_name":"AbTrivia","article_modified_time":"2025-12-25T22:20:29+00:00","twitter_card":"summary_large_image","schema":{"@context":"https:\/\/schema.org","@graph":[{"@type":"WebPage","@id":"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/","url":"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/","name":"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated - AbTrivia","isPartOf":{"@id":"https:\/\/abtriva.com\/cn\/#website"},"datePublished":"2025-12-25T22:20:27+00:00","dateModified":"2025-12-25T22:20:29+00:00","breadcrumb":{"@id":"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/#breadcrumb"},"inLanguage":"es_ES","potentialAction":[{"@type":"ReadAction","target":["https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/"]}]},{"@type":"BreadcrumbList","@id":"https:\/\/www.abtriva.com\/es\/product\/recombinant-human-activating-transcription-factor-7-interacting-protein-1-atf7ip-tuncated-acp16319\/#breadcrumb","itemListElement":[{"@type":"ListItem","position":1,"name":"Home","item":"https:\/\/www.abtriva.com\/es\/"},{"@type":"ListItem","position":2,"name":"Products","item":"https:\/\/www.abtriva.com\/es\/shop\/"},{"@type":"ListItem","position":3,"name":"Proteins","item":"https:\/\/www.abtriva.com\/es\/category\/proteins\/"},{"@type":"ListItem","position":4,"name":"Recombinant Proteins","item":"https:\/\/www.abtriva.com\/es\/category\/proteins\/recombinant-proteins\/"},{"@type":"ListItem","position":5,"name":"Recombinant Human Activating transcription factor 7-interacting protein 1 (ATF7IP), Truncated"}]},{"@type":"WebSite","@id":"https:\/\/abtriva.com\/cn\/#website","url":"https:\/\/abtriva.com\/cn\/","name":"AbTrivia","description":"","potentialAction":[{"@type":"SearchAction","target":{"@type":"EntryPoint","urlTemplate":"https:\/\/abtriva.com\/cn\/?s={search_term_string}"},"query-input":{"@type":"PropertyValueSpecification","valueRequired":true,"valueName":"search_term_string"}}],"inLanguage":"es_ES"}]}},"_links":{"self":[{"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/product\/123573","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/product"}],"about":[{"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/types\/product"}],"replies":[{"embeddable":true,"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/comments?post=123573"}],"wp:attachment":[{"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/media?parent=123573"}],"wp:term":[{"taxonomy":"product_brand","embeddable":true,"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/product_brand?post=123573"},{"taxonomy":"product_cat","embeddable":true,"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/product_cat?post=123573"},{"taxonomy":"product_tag","embeddable":true,"href":"https:\/\/www.abtriva.com\/es\/wp-json\/wp\/v2\/product_tag?post=123573"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}