{"id":111601,"date":"2025-12-25T14:48:28","date_gmt":"2025-12-25T14:48:28","guid":{"rendered":"https:\/\/advbiomart.sytech.site\/product\/recombinant-human-heme-oxygenase-1-hmox1-tuncated-acp04309\/"},"modified":"2025-12-25T14:48:29","modified_gmt":"2025-12-25T14:48:29","slug":"recombinant-human-heme-oxygenase-1-hmox1-tuncated-acp04309","status":"publish","type":"product","link":"https:\/\/www.abtriva.com\/cn\/product\/recombinant-human-heme-oxygenase-1-hmox1-tuncated-acp04309\/","title":{"rendered":"Recombinant Human Heme oxygenase 1 (HMOX1), Truncated"},"content":{"rendered":"","protected":false},"excerpt":{"rendered":"<p>The region for expressing recombinant Human HMOX1 contains amino acids 3-288. The theoretical molecular weight of the HMOX1 protein is 36.6 kDa. This HMOX1 protein is produced using e.coli expression system. The HMOX1 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant HMOX1 protein during the following stages.Human heme oxygenase 1 (HMOX1) is a crucial enzyme that plays a central role in heme catabolism. It catalyzes the degradation of heme into biliverdin, carbon monoxide (CO), and ferrous iron. Biliverdin is subsequently converted into bilirubin, an antioxidant with anti-inflammatory properties. HMOX1 is induced by various stimuli, including oxidative stress, inflammation, and environmental factors. Its expression is regulated by the transcription factor NRF2, which binds to the antioxidant response element (ARE) in the HMOX1 promoter. The enzymatic products generated by HMOX1 have protective effects against oxidative stress and inflammation. Research on HMOX1 is extensive, exploring its implications in diverse areas such as cellular stress response, inflammation, immune regulation, and its potential therapeutic applications in conditions associated with oxidative damage.<\/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":[48918],"class_list":["post-111601","product","type-product","status-publish","product_cat-proteins","product_cat-recombinant-proteins","product_tag-hmox1","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 Heme oxygenase 1 (HMOX1), 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\/cn\/es\/product\/recombinant-human-heme-oxygenase-1-hmox1-tuncated-acp04309\/\" \/>\n<meta property=\"og:locale\" content=\"cn_CN\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Recombinant Human Heme oxygenase 1 (HMOX1), Truncated - AbTrivia\" \/>\n<meta property=\"og:description\" content=\"The region for expressing recombinant Human HMOX1 contains amino acids 3-288. The theoretical molecular weight of the HMOX1 protein is 36.6 kDa. This HMOX1 protein is produced using e.coli expression system. The HMOX1 gene fragment has been modified by fusing the N-terminal 6xHis tag, providing convenience in detecting and purifying the recombinant HMOX1 protein during the following stages.Human heme oxygenase 1 (HMOX1) is a crucial enzyme that plays a central role in heme catabolism. It catalyzes the degradation of heme into biliverdin, carbon monoxide (CO), and ferrous iron. Biliverdin is subsequently converted into bilirubin, an antioxidant with anti-inflammatory properties. HMOX1 is induced by various stimuli, including oxidative stress, inflammation, and environmental factors. Its expression is regulated by the transcription factor NRF2, which binds to the antioxidant response element (ARE) in the HMOX1 promoter. The enzymatic products generated by HMOX1 have protective effects against oxidative stress and inflammation. 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