{"product_id":"lactate-dehydrogenase-ldh-from-porcine-heart-350-u-mg","title":"Lactate Dehydrogenase (LDH) from Porcine Heart, 350 U\/mg","description":"\u003cdiv style=\"max-width:1400px; margin:0 auto; padding:40px 20px; font-family:'Open Sans',sans-serif; font-weight:300; background:#fff; color:#333; font-size:0.95rem; box-sizing:border-box;\"\u003e\n  \u003cdiv style=\"display:flex; flex-direction:column; gap:20px;\"\u003e\n\u003ch2 style=\"margin:0; font-weight:600;\"\u003eLactate Dehydrogenase (LDH) from Porcine Heart, 350 U\/mg – Catalog #B2026857\u003c\/h2\u003e\n\u003cp\u003eLactate Dehydrogenase (LDH; EC 1.1.1.27) from porcine heart (Catalog #B2026857) is supplied as 1 kU of enzyme in solution with a specific activity of 350 U\/mg. LDH catalyzes the reversible interconversion of pyruvate and L-lactate with concomitant oxidation or reduction of NADH\/NAD⁺. Because the reaction can be followed directly by the change in NADH absorbance at 340 nm, porcine heart LDH is widely used as a coupling enzyme in enzyme kinetics, metabolic assays, and teaching laboratories.\u003c\/p\u003e\n\u003cdiv style=\"overflow-x:auto; max-width:100%; margin-bottom:20px;\"\u003e\n\u003ctable style=\"width:100%; max-width:640px; border-collapse:collapse;\"\u003e\n\u003ctbody\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eCatalog number:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eB2026857\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eLot number:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eBatch dependent\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eExpiration Date:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eBatch dependent\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eAmount:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003e1 kU\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eSpecific activity:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003e350 U\/mg\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eMolecular Weight or Concentration:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eN\/A\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eSupplied as:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eSolution\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eSource:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003ePorcine (pig) heart\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eApplications:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eNADH-coupled enzyme assays (e.g., PK\/LDH ATPase and kinase assays), pyruvate and lactate determination, enzyme kinetics, isozyme studies, teaching laboratories\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eStorage:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003e−20°C\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eKeywords:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eLactate dehydrogenase, LDH, L-lactate dehydrogenase, L-lactate:NAD⁺ oxidoreductase, EC 1.1.1.27, porcine heart LDH, pig heart LDH, LDH-1, H4 isozyme\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eGrade:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eBiotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity \u0026gt;18 MΩ-cm) and are filtered through 0.22 um.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e\n\u003c\/div\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eScientific Overview\u003c\/h3\u003e\n\u003cp\u003eLDH is a tetrameric enzyme built from ~35 kDa subunits. In vertebrates, M-type (muscle) and H-type (heart) subunits assemble into isozymes with distinct kinetic and physicochemical properties. Heart tissue is dominated by the H-type isozyme (H4, LDH-1), and the three-dimensional structure of pig heart H4 LDH was one of the first dehydrogenase structures to be solved and correlated with isozyme sequence differences. The enzyme catalyzes:\u003c\/p\u003e\n\u003cp\u003ePyruvate + NADH + H⁺ ⇌ L-Lactate + NAD⁺\u003c\/p\u003e\n\u003cp\u003eBecause NADH absorbs strongly at 340 nm (ε ≈ 6,220 M⁻¹cm⁻¹) and NAD⁺ does not, LDH turns any reaction that produces pyruvate into a simple, continuous spectrophotometric readout. The most common example is the pyruvate kinase\/LDH (PK\/LDH) coupled assay, where ADP produced by an ATPase or kinase is recycled by pyruvate kinase and the resulting pyruvate is reduced by LDH.\u003c\/p\u003e\n\u003cp\u003eKey applications include:\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003eCoupling enzyme for continuous NADH-linked assays (PK\/LDH ATPase and kinase assays)\u003c\/li\u003e\n\u003cli\u003eEnzymatic determination of pyruvate or L-lactate\u003c\/li\u003e\n\u003cli\u003eSteady-state enzyme kinetics and teaching laboratory exercises\u003c\/li\u003e\n\u003cli\u003eComparative studies of H- and M-type LDH isozymes\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eUsage \u0026amp; Handling Guidance\u003c\/h3\u003e\n\u003cp\u003eStore at −20°C as supplied. Thaw on ice, mix gently (do not vortex), and keep on ice during use. Dilute into cold assay buffer immediately before use and prepare aliquots to avoid repeated freeze–thaw cycles.\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e\n\u003cstrong\u003eDetection:\u003c\/strong\u003e Follow NADH oxidation or formation at 340 nm.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCoupled assays:\u003c\/strong\u003e Supply LDH in sufficient excess that it is never rate-limiting; confirm by showing the observed rate does not change when LDH is increased.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eUnit definition:\u003c\/strong\u003e Unit definitions differ between suppliers (temperature, pH, direction of reaction). Request the COA\/TDS for the lot-specific definition before converting units to mass.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eWhat You Get\u003c\/h3\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e1 kU of Lactate Dehydrogenase from porcine heart, supplied in solution\u003c\/li\u003e\n\u003cli\u003eSpecific activity of 350 U\/mg\u003c\/li\u003e\n\u003cli\u003eA convenient working quantity for assay development and routine coupled assays\u003c\/li\u003e\n\u003cli\u003eFor research use only (RUO)\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eWhy Researchers Choose It\u003c\/h3\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003eHigh specific activity for use as a non-rate-limiting coupling enzyme\u003c\/li\u003e\n\u003cli\u003eWell-characterized heart (H-type) enzyme with decades of structural and kinetic literature\u003c\/li\u003e\n\u003cli\u003eSimple 340 nm readout compatible with standard spectrophotometers and plate readers\u003c\/li\u003e\n\u003cli\u003eReady-to-use solution format\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eFrequently Asked Questions (FAQ)\u003c\/h3\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e\n\u003cstrong\u003eWhat reaction does LDH catalyze?\u003c\/strong\u003e\u003cbr\u003eThe reversible reduction of pyruvate to L-lactate using NADH, producing NAD⁺.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eHow is LDH used in a PK\/LDH coupled assay?\u003c\/strong\u003e\u003cbr\u003ePyruvate kinase converts ADP and phosphoenolpyruvate to ATP and pyruvate; LDH then reduces the pyruvate while oxidizing NADH, so ATP hydrolysis is read as a decrease in absorbance at 340 nm.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWhy porcine heart LDH rather than muscle LDH?\u003c\/strong\u003e\u003cbr\u003eHeart tissue provides mainly the H-type (LDH-1) isozyme, which differs kinetically from the muscle (M-type) form. Choose the isozyme that matches your assay conditions or the published method you are following.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eHow should I store it?\u003c\/strong\u003e\u003cbr\u003eAt −20°C. Aliquot to avoid repeated freeze–thaw cycles and keep on ice while working.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCan I get a COA or TDS?\u003c\/strong\u003e\u003cbr\u003eYes. Request a quote or contact us and we will provide available lot documentation.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cdiv style=\"margin-top:20px; font-weight:bold; color:#c8102e;\"\u003eThis product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use in humans or animals.\u003c\/div\u003e\n\u003chr\u003e\n\u003ch4\u003eReferences\u003c\/h4\u003e\n\u003cul style=\"padding-left:0; margin:0; list-style:none;\"\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eEventoff W, Rossmann MG, Taylor SS, Torff HJ, Meyer H, Keil W, Kiltz HH. Structural adaptations of lactate dehydrogenase isozymes. \u003cem\u003eProc Natl Acad Sci U S A.\u003c\/em\u003e 1977;74(7):2677-2681.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1073\/pnas.74.7.2677\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eEventoff W, Hackert ML, Rossmann MG. A low-resolution crystallographic study of porcine heart lactate dehydrogenase. \u003cem\u003eJ Mol Biol.\u003c\/em\u003e 1975;98(1):249-258.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1016\/s0022-2836(75)80113-6\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eGrau UM, Trommer WE, Rossmann MG. Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 Å resolution. \u003cem\u003eJ Mol Biol.\u003c\/em\u003e 1981;151(2):289-307.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1016\/0022-2836(81)90516-7\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eKiltz HH, Keil W, Griesbach M, Petry K, Meyer H. The primary structure of porcine lactate dehydrogenase: isoenzymes M4 and H4. \u003cem\u003eHoppe Seylers Z Physiol Chem.\u003c\/em\u003e 1977;358(1):123-127.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1515\/bchm2.1977.358.1.123\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eCahn RD, Zwilling E, Kaplan NO, Levine L. Nature and Development of Lactic Dehydrogenases: The two major types of this enzyme form molecular hybrids which change in makeup during development. \u003cem\u003eScience.\u003c\/em\u003e 1962;136(3520):962-9.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1126\/science.136.3520.962\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eRead JA, Winter VJ, Eszes CM, Sessions RB, Brady RL. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. \u003cem\u003eProteins.\u003c\/em\u003e 2001;43(2):175-185.\u003c\/span\u003e\u003ca href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/11276087\/\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n  \u003c\/div\u003e\n\u003c\/div\u003e","brand":"Molecular Depot","offers":[{"title":"Default Title","offer_id":52805515772202,"sku":"BTS-B2026857","price":1055.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/B2026857.png?v=1790798372","url":"https:\/\/bluetigerscientific.com\/products\/lactate-dehydrogenase-ldh-from-porcine-heart-350-u-mg","provider":"Blue Tiger Scientific","version":"1.0","type":"link"}