{"product_id":"proteinase-k-eq023","title":"Proteinase K","description":"\u003cp\u003eProteinase K\u003c\/p\u003e\n\u003ch4 class=\"tit clearfix tabs\"\u003e\u003cspan class=\"fz20 fl tran300 active\"\u003eOverview\u003c\/span\u003e\u003c\/h4\u003e\n\u003cdiv class=\"cont fz16 pageStyle\"\u003e\n\u003cdiv id=\"tabs-container\" class=\"container1 swiper-container-horizontal swiper-container-autoheight\"\u003e\n\u003cdiv class=\"swiper-wrapper\"\u003e\n\u003cdiv class=\"swiper-slide pageStyle fz16 swiper-no-swiping swiper-slide-active\"\u003e\n\u003ctable class=\"table2\"\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd width=\"208px\" class=\"fz18\"\u003eProduct name:\u003c\/td\u003e\n\u003ctd\u003eProteinase K\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd class=\"fz18\"\u003eIntroduction:\u003c\/td\u003e\n\u003ctd\u003eProteinase K is a serine protease that belongs to the subtilisin family. It has extremely high enzyme activity and wide substrate specificity. It can preferentially decompose the ester bonds and peptide bonds adjacent to the C-terminus of hydrophobic amino acids, sulfur-containing amino acids, and aromatic amino acids. It is often used to degrade proteins to produce short peptides. It has the typical catalytic triad Asp39-His69-Ser224 characteristics unique to serine proteases, and there are two Ca2+ binding sites around the active center to increase its stability, allowing it to maintain high enzyme activity under more extensive conditions.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"ELK Biotechnology","offers":[{"title":"1mL","offer_id":42135282745568,"sku":"EQ023","price":200.0,"currency_code":"KRW","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0601\/9330\/8896\/products\/ELK_4899bfd4-c402-45c5-9aaf-7a98d21e345e.jpg?v=1638297985","url":"https:\/\/rndmate.com\/products\/proteinase-k-eq023","provider":"알앤디메이트","version":"1.0","type":"link"}