{"title":"Fibrinogen \/ D-Dimer \/ Thrombin","description":null,"products":[{"product_id":"human-tissue-factor-f3-elisa-kit-ez-set-diy-antibody-pairs-bhe21000020","title":"Human Tissue Factor\/F3 ELISA Kit EZ-Set™ (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tissue factor, TF, Coagulation factor III, Thromboplastin, CD142, F3.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eTissue Factor\/F3\u003c\/strong\u003e (\u003cstrong\u003eF3\u003c\/strong\u003e) is an established target in many assay panels, supporting hypothesis testing across diverse biological systems. This target is frequently investigated in \u003cstrong\u003eOncology \u0026amp; Angiogenesis\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003ecell-surface signaling and cell-state markers\u003c\/strong\u003e. Many receptors and surface markers act as gateways for signaling or as phenotypic indicators of specific cell populations and activation states.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. Interpreting changes benefits from considering compartment (cell-associated vs soluble), the time scale of regulation, and whether complexes or modified forms contribute to the measured signal.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSystems-level readout:\u003c\/strong\u003e Quantification supports comparisons across conditions, time points, and treatment groups.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic interpretation:\u003c\/strong\u003e Pairing with upstream regulators and downstream markers helps contextualize changes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker-style profiling:\u003c\/strong\u003e Measuring panels of related analytes can improve interpretability in complex models.\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Boster Bio","offers":[{"title":"5 plates\/kit","offer_id":52920801853805,"sku":"EZ0928","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0928-2-ELISA-human-tissue-factor-f3-ez-set-elisa-kit-diy-antibody-pairs.jpg?v=1769077475"},{"product_id":"human-angiostatin-k1-3-elisa-kit-ez-set-diy-antibody-pairs-bhe21000067","title":"Human Angiostatin K1-3 ELISA Kit EZ-Set™ (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Plasminogen, Plasmin heavy chain A, Activation peptide, Angiostatin, short form, Plasmin light chain B, PLG.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eAngiostatin K1-3\u003c\/strong\u003e (\u003cstrong\u003ePLG\u003c\/strong\u003e) is an established target in many assay panels, supporting hypothesis testing across diverse biological systems. This target is frequently investigated in \u003cstrong\u003eImmunology \u0026amp; Inflammation\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"5 plates\/kit","offer_id":52920803393901,"sku":"EZ0905","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0905.jpg?v=1769077492"},{"product_id":"human-plat-tpa-elisa-kit-ez-set-diy-antibody-pairs-bhe21000071","title":"Human PLAT\/TPA ELISA Kit EZ-Set™ (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tissue-type plasminogen activator, t-PA, t-plasminogen activator, tPA, Alteplase, Reteplase, Tissue-type plasminogen activator chain A, Tissue-type plasminogen activator chain B.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePLAT\/TPA\u003c\/strong\u003e (\u003cstrong\u003ePLAT\u003c\/strong\u003e) is widely studied as a molecular readout in experimental models where changes in protein abundance reflect underlying biology. This target is frequently investigated in \u003cstrong\u003eBone \u0026amp; Musculoskeletal\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"5 plates\/kit","offer_id":52920803557741,"sku":"EZ0897","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0897_ed7451e9-5ca0-42d5-a256-e2e60948a630.jpg?v=1769077493"},{"product_id":"human-angiostatin-kringle-1-3-plg-picokine-quick-elisa-kit-bhe21000148","title":"Human Angiostatin Kringle 1-3\/PLG PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Plasminogen, 3.4.21.7, Plasmin heavy chain A, Activation peptide, Angiostatin, short form, Plasmin light chain B, PLG.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eAngiostatin Kringle 1-3\/PLG\u003c\/strong\u003e (\u003cstrong\u003ePLG\u003c\/strong\u003e) is an established target in many assay panels, supporting hypothesis testing across diverse biological systems. This target is frequently investigated in \u003cstrong\u003eMetabolism \u0026amp; Diabetes\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920806048109,"sku":"FEK0905","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/fek0905_1_bc7197c4-4fd1-49e1-bb6a-027b64b64f78.png?v=1769077526"},{"product_id":"human-plat-tpa-picokine-quick-elisa-kit-bhe21000164","title":"Human PLAT\/TPA PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tissue-type plasminogen activator, t-PA, t-plasminogen activator, tPA, 3.4.21.68, Alteplase, Reteplase, Tissue-type plasminogen activator chain A.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePLAT\/TPA\u003c\/strong\u003e (\u003cstrong\u003ePLAT\u003c\/strong\u003e) is widely studied as a molecular readout in experimental models where changes in protein abundance reflect underlying biology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920806637933,"sku":"FEK0897","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0897_0759b435-6985-49b8-9bbb-cbcf333ea47d.png?v=1769077533"},{"product_id":"human-serpin-c1-antithrombin-iii-picokine-quick-elisa-kit-bhe21000213","title":"Human Serpin C1\/Antithrombin-III PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Antithrombin-III, ATIII, Serpin C1, SERPINC1, AT3, PRO0309.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eSerpin C1\/Antithrombin-III\u003c\/strong\u003e (\u003cstrong\u003eSERPINC1\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eECM \u0026amp; Cell Adhesion\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920808276333,"sku":"FEK1393","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1393-ELISA-human-serpin-c1-antithrombin-iii-picokine-elisa-kit_92e0fe60-9a5d-4e75-aaff-114c11a3cb15.png?v=1769077553"},{"product_id":"human-pai-1-elisa-kit-picokine-bhe21000664","title":"Human PAI-1 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Plasminogen activator inhibitor 1, PAI, PAI-1, Endothelial plasminogen activator inhibitor, Serpin E1, SERPINE1, PAI1, PLANH1.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePAI-1\u003c\/strong\u003e (\u003cstrong\u003eSERPINE1\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920824070509,"sku":"EK0859","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0859.png?v=1769077791"},{"product_id":"human-plat-tpa-elisa-kit-picokine-bhe21000680","title":"Human PLAT\/TPA ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tissue-type plasminogen activator, t-PA, t-plasminogen activator, tPA, 3.4.21.68, Alteplase, Reteplase, Tissue-type plasminogen activator chain A.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePLAT\/TPA\u003c\/strong\u003e (\u003cstrong\u003ePLAT\u003c\/strong\u003e) is widely studied as a molecular readout in experimental models where changes in protein abundance reflect underlying biology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920824594797,"sku":"EK0897","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0897_803d5b28-a68f-4f85-b1c4-b9ea98753676.png?v=1769077800"},{"product_id":"human-angiostatin-kringle-1-3-plg-elisa-kit-picokine-bhe21000686","title":"Human Angiostatin Kringle 1-3\/PLG ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Plasminogen, 3.4.21.7, Plasmin heavy chain A, Activation peptide, Angiostatin, short form, Plasmin light chain B, PLG.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eAngiostatin Kringle 1-3\/PLG\u003c\/strong\u003e (\u003cstrong\u003ePLG\u003c\/strong\u003e) is an established target in many assay panels, supporting hypothesis testing across diverse biological systems. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920825184621,"sku":"EK0905","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0905.png?v=1769077804"},{"product_id":"human-thrombomodulin-elisa-kit-picokine-bhe21000694","title":"Human Thrombomodulin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Thrombomodulin, TM, Fetomodulin, CD141, THBD, THRM.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eThrombomodulin\u003c\/strong\u003e (\u003cstrong\u003eTHBD\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003ecell-surface signaling and cell-state markers\u003c\/strong\u003e. Many receptors and surface markers act as gateways for signaling or as phenotypic indicators of specific cell populations and activation states.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. Interpreting changes benefits from considering compartment (cell-associated vs soluble), the time scale of regulation, and whether complexes or modified forms contribute to the measured signal.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSystems-level readout:\u003c\/strong\u003e Quantification supports comparisons across conditions, time points, and treatment groups.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic interpretation:\u003c\/strong\u003e Pairing with upstream regulators and downstream markers helps contextualize changes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker-style profiling:\u003c\/strong\u003e Measuring panels of related analytes can improve interpretability in complex models.\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920825446765,"sku":"EK0917","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0917.png?v=1769077806"},{"product_id":"human-tissue-factor-f3-elisa-kit-picokine-bhe21000702","title":"Human Tissue Factor\/F3 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tissue factor, TF, Coagulation factor III, Thromboplastin, CD142, F3.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eTissue Factor\/F3\u003c\/strong\u003e (\u003cstrong\u003eF3\u003c\/strong\u003e) is an established target in many assay panels, supporting hypothesis testing across diverse biological systems. This target is frequently investigated in \u003cstrong\u003eMetabolism \u0026amp; Diabetes\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003ecell-surface signaling and cell-state markers\u003c\/strong\u003e. Many receptors and surface markers act as gateways for signaling or as phenotypic indicators of specific cell populations and activation states.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. Interpreting changes benefits from considering compartment (cell-associated vs soluble), the time scale of regulation, and whether complexes or modified forms contribute to the measured signal.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSystems-level readout:\u003c\/strong\u003e Quantification supports comparisons across conditions, time points, and treatment groups.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic interpretation:\u003c\/strong\u003e Pairing with upstream regulators and downstream markers helps contextualize changes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker-style profiling:\u003c\/strong\u003e Measuring panels of related analytes can improve interpretability in complex models.\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920825708909,"sku":"EK0928","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0928_12c8c354-3f3e-4cab-bfa0-3ec694a52930.png?v=1769077809"},{"product_id":"mouse-thrombomodulin-elisa-kit-picokine-bhe21000773","title":"Mouse Thrombomodulin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Thrombomodulin, TM, Fetomodulin, CD141, Thbd.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eThrombomodulin\u003c\/strong\u003e (\u003cstrong\u003eTHBD\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003ecell-surface signaling and cell-state markers\u003c\/strong\u003e. Many receptors and surface markers act as gateways for signaling or as phenotypic indicators of specific cell populations and activation states.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. Interpreting changes benefits from considering compartment (cell-associated vs soluble), the time scale of regulation, and whether complexes or modified forms contribute to the measured signal.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSystems-level readout:\u003c\/strong\u003e Quantification supports comparisons across conditions, time points, and treatment groups.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic interpretation:\u003c\/strong\u003e Pairing with upstream regulators and downstream markers helps contextualize changes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker-style profiling:\u003c\/strong\u003e Measuring panels of related analytes can improve interpretability in complex models.\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920828625261,"sku":"EK1119","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1119_8cce21e2-14f9-427c-b57d-afc50df84f4b.png?v=1769077844"},{"product_id":"mouse-tissue-factor-f3-elisa-kit-picokine-bhe21000958","title":"Mouse Tissue Factor\/F3 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tissue factor, TF, Coagulation factor III, CD142, F3, Cf-3, Cf3.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eTissue Factor\/F3\u003c\/strong\u003e (\u003cstrong\u003eF3\u003c\/strong\u003e) is an established target in many assay panels, supporting hypothesis testing across diverse biological systems. This target is frequently investigated in \u003cstrong\u003eCell Signaling\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003ecell-surface signaling and cell-state markers\u003c\/strong\u003e. Many receptors and surface markers act as gateways for signaling or as phenotypic indicators of specific cell populations and activation states.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. Interpreting changes benefits from considering compartment (cell-associated vs soluble), the time scale of regulation, and whether complexes or modified forms contribute to the measured signal.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSystems-level readout:\u003c\/strong\u003e Quantification supports comparisons across conditions, time points, and treatment groups.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic interpretation:\u003c\/strong\u003e Pairing with upstream regulators and downstream markers helps contextualize changes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker-style profiling:\u003c\/strong\u003e Measuring panels of related analytes can improve interpretability in complex models.\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920836424045,"sku":"EK1367","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1367_1.png?v=1769077952"},{"product_id":"human-serpin-c1-antithrombin-iii-elisa-kit-picokine-bhe21000992","title":"Human Serpin C1\/Antithrombin-III ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Antithrombin-III, ATIII, Serpin C1, SERPINC1, AT3, PRO0309.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eSerpin C1\/Antithrombin-III\u003c\/strong\u003e (\u003cstrong\u003eSERPINC1\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920839602541,"sku":"EK1393","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1393.jpg?v=1769077975"},{"product_id":"monkey-primate-thrombomodulin-elisa-kit-picokine-bhe21001248","title":"Monkey primate Thrombomodulin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Thrombomodulin, TM, Fetomodulin, CD141, THBD, THRM.\u003c\/p\u003e\u003cp\u003eMonkey \u003cstrong\u003eprimate Thrombomodulin\u003c\/strong\u003e (\u003cstrong\u003eTHBD\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eRenal \u0026amp; Urology\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003ecell-surface signaling and cell-state markers\u003c\/strong\u003e. Many receptors and surface markers act as gateways for signaling or as phenotypic indicators of specific cell populations and activation states.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. Interpreting changes benefits from considering compartment (cell-associated vs soluble), the time scale of regulation, and whether complexes or modified forms contribute to the measured signal.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSystems-level readout:\u003c\/strong\u003e Quantification supports comparisons across conditions, time points, and treatment groups.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic interpretation:\u003c\/strong\u003e Pairing with upstream regulators and downstream markers helps contextualize changes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker-style profiling:\u003c\/strong\u003e Measuring panels of related analytes can improve interpretability in complex models.\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920862343533,"sku":"EK0917-PR","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0917-pr.png?v=1769078123"},{"product_id":"human-vwf-a2-vwf-elisa-kit-picokine-bhe21001386","title":"Human VWF-A2\/VWF ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e von Willebrand factor, vWF, von Willebrand antigen 2, von Willebrand antigen II, F8VWF.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eVWF-A2\/VWF\u003c\/strong\u003e (\u003cstrong\u003eVWF\u003c\/strong\u003e) is widely studied as a molecular readout in experimental models where changes in protein abundance reflect underlying biology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003eplasma protein and inflammation-linked pathways\u003c\/strong\u003e. Inflammation and coagulation networks include abundant plasma proteins, regulators, and cleavage products that can change with immune activation and tissue damage.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. Interpreting changes benefits from considering compartment (cell-associated vs soluble), the time scale of regulation, and whether complexes or modified forms contribute to the measured signal.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eSystems-level readout:\u003c\/strong\u003e Quantification supports comparisons across conditions, time points, and treatment groups.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic interpretation:\u003c\/strong\u003e Pairing with upstream regulators and downstream markers helps contextualize changes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eBiomarker-style profiling:\u003c\/strong\u003e Measuring panels of related analytes can improve interpretability in complex models.\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920874271085,"sku":"EK1743","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1743.jpg?v=1769078186"},{"product_id":"human-pros1-protein-s-elisa-kit-picokine-bhe21001390","title":"Human PROS1 \/ Protein S ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Vitamin K-dependent protein S, PROS1, PROS.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePROS1 \/ Protein S\u003c\/strong\u003e (\u003cstrong\u003ePROS1\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. As with many protein targets, abundance can be influenced by transcriptional regulation, secretion or shedding, proteolytic processing, and clearance. Quantitative measurement is often used to connect molecular changes with phenotypes such as stress responses, immune activation, differentiation, or tissue remodeling.\u003c\/p\u003e\u003ch2\u003eBiological context and interpretation\u003c\/h2\u003e\u003cp\u003eProtein-level readouts complement nucleic-acid measurements by reflecting post-transcriptional control and protein stability. Depending on the model system, changes may be transient or sustained, and may represent direct pathway engagement or secondary effects. When interpreting results, consider sample matrix effects, timing relative to stimulation or treatment, and whether complexes or modified forms of the analyte may be present.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eComparative quantification:\u003c\/strong\u003e Supports analysis across experimental groups, time points, or dose ranges.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePathway context:\u003c\/strong\u003e Useful as part of a broader marker panel to triangulate biological mechanisms.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eModel characterization:\u003c\/strong\u003e Helps profile baseline vs perturbed states in cells, tissues, or biofluids.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eRelated pathways and interacting partners\u003c\/h2\u003e\u003cp\u003eFor many targets, interpretability improves when measured alongside biologically connected markers (e.g., upstream regulators, downstream effectors, and cell-type indicators). Designing panels around a pathway hypothesis can help distinguish primary pathway activation from general stress or inflammation.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920874402157,"sku":"EK1739","price":750.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1739.jpg?v=1769078188"},{"product_id":"human-proc-protein-c-elisa-kit-picokine-bhe21001476","title":"Human PROC\/Protein C ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Vitamin K-dependent protein C, Anticoagulant protein C, Autoprothrombin IIA, Blood coagulation factor XIV, Proc.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePROC\/Protein C\u003c\/strong\u003e (\u003cstrong\u003eProc\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eCell Signaling\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920877547885,"sku":"EK1975","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1975.jpg?v=1769078241"},{"product_id":"human-f7-elisa-kit-picokine-bhe21001742","title":"Human F7 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003eHuman \u003cstrong\u003eF7\u003c\/strong\u003e (\u003cstrong\u003eF7\u003c\/strong\u003e) is an established target in many assay panels, supporting hypothesis testing across diverse biological systems. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. As with many protein targets, abundance can be influenced by transcriptional regulation, secretion or shedding, proteolytic processing, and clearance. Quantitative measurement is often used to connect molecular changes with phenotypes such as stress responses, immune activation, differentiation, or tissue remodeling.\u003c\/p\u003e\u003ch2\u003eBiological context and interpretation\u003c\/h2\u003e\u003cp\u003eProtein-level readouts complement nucleic-acid measurements by reflecting post-transcriptional control and protein stability. Depending on the model system, changes may be transient or sustained, and may represent direct pathway engagement or secondary effects. When interpreting results, consider sample matrix effects, timing relative to stimulation or treatment, and whether complexes or modified forms of the analyte may be present.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eComparative quantification:\u003c\/strong\u003e Supports analysis across experimental groups, time points, or dose ranges.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePathway context:\u003c\/strong\u003e Useful as part of a broader marker panel to triangulate biological mechanisms.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eModel characterization:\u003c\/strong\u003e Helps profile baseline vs perturbed states in cells, tissues, or biofluids.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eRelated pathways and interacting partners\u003c\/h2\u003e\u003cp\u003eFor many targets, interpretability improves when measured alongside biologically connected markers (e.g., upstream regulators, downstream effectors, and cell-type indicators). Designing panels around a pathway hypothesis can help distinguish primary pathway activation from general stress or inflammation.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920895439213,"sku":"EK2197","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek2197.jpg?v=1769078371"},{"product_id":"human-f10-elisa-kit-picokine-bhe21001743","title":"Human F10 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003eHuman \u003cstrong\u003eF10\u003c\/strong\u003e (\u003cstrong\u003eF10\u003c\/strong\u003e) is widely studied as a molecular readout in experimental models where changes in protein abundance reflect underlying biology. This target is frequently investigated in \u003cstrong\u003eOncology \u0026amp; Angiogenesis\u003c\/strong\u003e research contexts. As with many protein targets, abundance can be influenced by transcriptional regulation, secretion or shedding, proteolytic processing, and clearance. Quantitative measurement is often used to connect molecular changes with phenotypes such as stress responses, immune activation, differentiation, or tissue remodeling.\u003c\/p\u003e\u003ch2\u003eBiological context and interpretation\u003c\/h2\u003e\u003cp\u003eProtein-level readouts complement nucleic-acid measurements by reflecting post-transcriptional control and protein stability. Depending on the model system, changes may be transient or sustained, and may represent direct pathway engagement or secondary effects. 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Designing panels around a pathway hypothesis can help distinguish primary pathway activation from general stress or inflammation.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920895471981,"sku":"EK2198","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek2198.jpg?v=1769078371"},{"product_id":"human-f11-elisa-kit-picokine-bhe21001744","title":"Human F11 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003eHuman \u003cstrong\u003eF11\u003c\/strong\u003e (\u003cstrong\u003eF11\u003c\/strong\u003e) is widely studied as a molecular readout in experimental models where changes in protein abundance reflect underlying biology. This target is frequently investigated in \u003cstrong\u003eImmunology \u0026amp; Inflammation\u003c\/strong\u003e research contexts. As with many protein targets, abundance can be influenced by transcriptional regulation, secretion or shedding, proteolytic processing, and clearance. Quantitative measurement is often used to connect molecular changes with phenotypes such as stress responses, immune activation, differentiation, or tissue remodeling.\u003c\/p\u003e\u003ch2\u003eBiological context and interpretation\u003c\/h2\u003e\u003cp\u003eProtein-level readouts complement nucleic-acid measurements by reflecting post-transcriptional control and protein stability. Depending on the model system, changes may be transient or sustained, and may represent direct pathway engagement or secondary effects. When interpreting results, consider sample matrix effects, timing relative to stimulation or treatment, and whether complexes or modified forms of the analyte may be present.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eComparative quantification:\u003c\/strong\u003e Supports analysis across experimental groups, time points, or dose ranges.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePathway context:\u003c\/strong\u003e Useful as part of a broader marker panel to triangulate biological mechanisms.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eModel characterization:\u003c\/strong\u003e Helps profile baseline vs perturbed states in cells, tissues, or biofluids.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eRelated pathways and interacting partners\u003c\/h2\u003e\u003cp\u003eFor many targets, interpretability improves when measured alongside biologically connected markers (e.g., upstream regulators, downstream effectors, and cell-type indicators). Designing panels around a pathway hypothesis can help distinguish primary pathway activation from general stress or inflammation.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920895504749,"sku":"EK2199","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek2199.jpg?v=1769078371"},{"product_id":"human-serpin-c1-antithrombin-iii-ez-set-and-trade-elisa-kit-diy-antibody-pairs-bhe21002125","title":"Human Serpin C1\/Antithrombin-III EZ-Set\u0026trade; ELISA Kit (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Antithrombin-III, ATIII, Serpin C1, SERPINC1, AT3, PRO0309.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eSerpin C1\/Antithrombin-III\u003c\/strong\u003e (\u003cstrong\u003eSERPINC1\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. Proteases and extracellular matrix (ECM) components are central to tissue architecture and remodeling. In many experimental contexts, changes in ECM-related proteins reflect shifts in cell adhesion, migration, barrier integrity, or matrix turnover.\u003c\/p\u003e\u003ch2\u003eBiological function and remodeling context\u003c\/h2\u003e\u003cp\u003eMatrix remodeling is influenced by the balance between synthesis and degradation, often regulated by inflammatory cues, mechanical stress, and growth-factor signaling. Protease activity can unmask or release bioactive fragments, while altered ECM composition can feed back on cell behavior through mechanotransduction and receptor engagement.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eRemodeling readout:\u003c\/strong\u003e Quantification can support studies of fibrosis, wound repair, and invasion models.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMicroenvironment state:\u003c\/strong\u003e Levels may reflect stromal activation, barrier disruption, or matrix turnover.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic linkage:\u003c\/strong\u003e Pairing with inflammatory and growth-factor markers can clarify drivers of remodeling.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eECM remodeling and protease regulation are frequently discussed in the literature across oncology, cardiovascular, pulmonary, and inflammatory disease models. Interpretation of abundance should consider whether the measured analyte represents pro-forms, active forms, or fragments, and whether binding partners in the matrix influence detectability.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"5 plates\/kit","offer_id":52920912478573,"sku":"EZ1393","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez1393_1dc446b0-f9db-484e-8f9a-b90f483938bc.png?v=1769078576"},{"product_id":"human-pros1-protein-s-ez-set-and-trade-elisa-kit-diy-antibody-pairs-bhe21002143","title":"Human PROS1\/Protein S EZ-Set\u0026trade; ELISA Kit (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Vitamin K-dependent protein S, PROS1, PROS.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePROS1\/Protein S\u003c\/strong\u003e (\u003cstrong\u003ePROS1\u003c\/strong\u003e) is a commonly measured biological analyte that can provide insight into cellular state and tissue physiology. This target is frequently investigated in \u003cstrong\u003eMolecular \u0026amp; Cellular Biology\u003c\/strong\u003e research contexts. As with many protein targets, abundance can be influenced by transcriptional regulation, secretion or shedding, proteolytic processing, and clearance. Quantitative measurement is often used to connect molecular changes with phenotypes such as stress responses, immune activation, differentiation, or tissue remodeling.\u003c\/p\u003e\u003ch2\u003eBiological context and interpretation\u003c\/h2\u003e\u003cp\u003eProtein-level readouts complement nucleic-acid measurements by reflecting post-transcriptional control and protein stability. Depending on the model system, changes may be transient or sustained, and may represent direct pathway engagement or secondary effects. When interpreting results, consider sample matrix effects, timing relative to stimulation or treatment, and whether complexes or modified forms of the analyte may be present.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eComparative quantification:\u003c\/strong\u003e Supports analysis across experimental groups, time points, or dose ranges.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003ePathway context:\u003c\/strong\u003e Useful as part of a broader marker panel to triangulate biological mechanisms.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eModel characterization:\u003c\/strong\u003e Helps profile baseline vs perturbed states in cells, tissues, or biofluids.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eRelated pathways and interacting partners\u003c\/h2\u003e\u003cp\u003eFor many targets, interpretability improves when measured alongside biologically connected markers (e.g., upstream regulators, downstream effectors, and cell-type indicators). Designing panels around a pathway hypothesis can help distinguish primary pathway activation from general stress or inflammation.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"5 plates\/kit","offer_id":52920913101165,"sku":"EZ1739","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez1739.png?v=1769078586"},{"product_id":"human-vwf-a2-vwf-ez-set-and-trade-elisa-kit-diy-antibody-pairs-bhe21002144","title":"Human VWF-A2\/VWF EZ-Set\u0026trade; ELISA Kit (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e von Willebrand factor, vWF, von Willebrand antigen 2, von Willebrand antigen II, F8VWF.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eVWF-A2\/VWF\u003c\/strong\u003e (\u003cstrong\u003eVWF\u003c\/strong\u003e) is widely studied as a molecular readout in experimental models where changes in protein abundance reflect underlying biology. This target is frequently investigated in \u003cstrong\u003eOncology \u0026amp; Angiogenesis\u003c\/strong\u003e research contexts. This analyte is often discussed in the context of \u003cstrong\u003eplasma protein and inflammation-linked pathways\u003c\/strong\u003e. Inflammation and coagulation networks include abundant plasma proteins, regulators, and cleavage products that can change with immune activation and tissue damage.\u003c\/p\u003e\u003ch2\u003eBiological context\u003c\/h2\u003e\u003cp\u003eIn experimental systems, protein abundance can reflect regulated expression, secretion, processing, or clearance. 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This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P13909\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Plasminogen Activator Inhibitor 1 (SERPINE1) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Plasminogen Activator Inhibitor 1 (SERPINE1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003ePlasminogen Activator Inhibitor 1 (SERPINE1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Plasminogen Activator Inhibitor 1 (SERPINE1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePlasminogen Activator Inhibitor 1 (SERPINE1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eEndothelial plasminogen activator inhibitor\u003c\/strong\u003e, \u003cstrong\u003ePAI\u003c\/strong\u003e, and \u003cstrong\u003ePAI-1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952445485421,"sku":"E0115Bo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0115Bo.jpg?v=1769145920"},{"product_id":"bovine-anti-thrombin-3-at-3-elisa-kit-bhe12100205","title":"Bovine Anti-Thrombin 3, AT-3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAnti-Thrombin 3 (SERPINC1)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P41361\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Anti-Thrombin 3 (SERPINC1) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Anti-Thrombin 3 (SERPINC1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eAnti-Thrombin 3 (SERPINC1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Anti-Thrombin 3 (SERPINC1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAnti-Thrombin 3 (SERPINC1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAntithrombin-III\u003c\/strong\u003e, \u003cstrong\u003eAT3\u003c\/strong\u003e, and \u003cstrong\u003eATIII\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952445976941,"sku":"E0195Bo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0195Bo.jpg?v=1769145924"},{"product_id":"canine-von-willebrand-factor-vwf-elisa-kit-bhe12100575","title":"Canine Von Willebrand Factor, VWF ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVon Willebrand Factor (VWF)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q28295\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Von Willebrand Factor (VWF) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Von Willebrand Factor (VWF) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eVon Willebrand Factor (VWF) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Von Willebrand Factor (VWF) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVon Willebrand Factor (VWF)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003evon Willebrand factor\u003c\/strong\u003e and \u003cstrong\u003evWF\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952449941869,"sku":"E0022Ca-96T","price":475.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0022Ca.jpg?v=1769145961"},{"product_id":"canine-coagulation-factor-5-f5-elisa-kit-bhe12100788","title":"Canine Coagulation Factor 5, F5 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF8\u003c\/strong\u003e is a molecular target commonly studied in life science research. 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Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eF8 has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of F8 can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF8\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCoagulation factor VIII\u003c\/strong\u003e, \u003cstrong\u003eF8\u003c\/strong\u003e, and \u003cstrong\u003eProcoagulant component\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952450695533,"sku":"E0275Ca-96T","price":475.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0275Ca.jpg?v=1769145966"},{"product_id":"canine-coagulation-factor-9-f9-elisa-kit-bhe12100790","title":"Canine Coagulation Factor 9, F9 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF9\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular and immunology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P19540\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, F9 is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of F9 can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eF9 has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of F9 can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF9\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eChristmas factor\u003c\/strong\u003e, \u003cstrong\u003eCoagulation factor IX\u003c\/strong\u003e, and \u003cstrong\u003eCoagulation factor IXa heavy chain\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952450728301,"sku":"E0277Ca-96T","price":475.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0277Ca.jpg?v=1769145966"},{"product_id":"chicken-fibrinogen-fbg-elisa-kit-bhe12101152","title":"Chicken Fibrinogen, FBG ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibrinogen (FN1)\u003c\/strong\u003e is a molecular target commonly studied in life science research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P11722\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibrinogen (FN1) is frequently examined in relation to mechanistic biology studies, biomarker-focused profiling, and disease-model research. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Fibrinogen (FN1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eFibrinogen (FN1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Fibrinogen (FN1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibrinogen (FN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eFibronectin\u003c\/strong\u003e, \u003cstrong\u003eFN\u003c\/strong\u003e, and \u003cstrong\u003eFN 1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952452858221,"sku":"E0245Ch-96T","price":498.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0245Ch.jpg?v=1769145984"},{"product_id":"human-placental-thrombin-inhibitor-pti-elisa-kit-bhe12102476","title":"Human Placental Thrombin Inhibitor, PTI ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePlacental Thrombin Inhibitor (SERPINB6)\u003c\/strong\u003e is a molecular target commonly studied in life science research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P35237\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Placental Thrombin Inhibitor (SERPINB6) is frequently examined in relation to mechanistic biology studies, biomarker-focused profiling, and disease-model research. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Placental Thrombin Inhibitor (SERPINB6) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003ePlacental Thrombin Inhibitor (SERPINB6) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Placental Thrombin Inhibitor (SERPINB6) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePlacental Thrombin Inhibitor (SERPINB6)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCAP\u003c\/strong\u003e, \u003cstrong\u003eCytoplasmic antiproteinase\u003c\/strong\u003e, and \u003cstrong\u003ePeptidase inhibitor 6\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952462492013,"sku":"E0797Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0797Hu.jpg?v=1769146084"},{"product_id":"human-prothrombin-pt-elisa-kit-bhe12102793","title":"Human Prothrombin, PT ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF2\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P00734\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, F2 is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of F2 can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eF2 has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of F2 can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF2\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eActivation Peptide fragment 1\u003c\/strong\u003e, \u003cstrong\u003eActivation Peptide fragment 2\u003c\/strong\u003e, and \u003cstrong\u003eCoagulation factor II\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952465375597,"sku":"E1146Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1146Hu.jpg?v=1769146115"},{"product_id":"human-plasminogen-activator-inhibitor-1-pai-1-elisa-kit-bhe12102806","title":"Human Plasminogen Activator Inhibitor 1, PAI-1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePlasminogen Activator Inhibitor 1 (SERPINE1)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P05121\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Plasminogen Activator Inhibitor 1 (SERPINE1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Plasminogen Activator Inhibitor 1 (SERPINE1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003ePlasminogen Activator Inhibitor 1 (SERPINE1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Plasminogen Activator Inhibitor 1 (SERPINE1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePlasminogen Activator Inhibitor 1 (SERPINE1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eEndothelial plasminogen activator inhibitor\u003c\/strong\u003e, \u003cstrong\u003ePAI\u003c\/strong\u003e, and \u003cstrong\u003ePAI-1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952465441133,"sku":"E1159Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1159Hu.jpg?v=1769146116"},{"product_id":"human-anti-thrombin-3-at-3-elisa-kit-bhe12102821","title":"Human Anti-Thrombin 3, AT-3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAnti-Thrombin 3 (SERPINC1)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P01008\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Anti-Thrombin 3 (SERPINC1) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Anti-Thrombin 3 (SERPINC1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eAnti-Thrombin 3 (SERPINC1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Anti-Thrombin 3 (SERPINC1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAnti-Thrombin 3 (SERPINC1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAntithrombin-III\u003c\/strong\u003e, \u003cstrong\u003eATIII\u003c\/strong\u003e, and \u003cstrong\u003eSerpin C1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952465506669,"sku":"E1174Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1174Hu.jpg?v=1769146116"},{"product_id":"human-thrombomodulin-tm-elisa-kit-bhe12102830","title":"Human Thrombomodulin, TM ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eThrombomodulin (THBD)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P07204\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Thrombomodulin (THBD) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Thrombomodulin (THBD) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eThrombomodulin (THBD) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Thrombomodulin (THBD) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eThrombomodulin (THBD)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCD antigen CD141\u003c\/strong\u003e, \u003cstrong\u003eFetomodulin\u003c\/strong\u003e, and \u003cstrong\u003eTHBD\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952465539437,"sku":"E1183Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1183Hu.jpg?v=1769146116"},{"product_id":"human-von-willebrand-factor-vwf-elisa-kit-bhe12102833","title":"Human Von Willebrand Factor, VWF ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVon Willebrand Factor (VWF)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P04275\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Von Willebrand Factor (VWF) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Von Willebrand Factor (VWF) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eVon Willebrand Factor (VWF) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Von Willebrand Factor (VWF) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVon Willebrand Factor (VWF)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003evon Willebrand antigen 2\u003c\/strong\u003e, \u003cstrong\u003evon Willebrand antigen II\u003c\/strong\u003e, and \u003cstrong\u003evon Willebrand factor\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952465572205,"sku":"E1186Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1186Hu.jpg?v=1769146117"},{"product_id":"human-tissue-factor-tf-elisa-kit-bhe12102841","title":"Human Tissue Factor, TF ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF3\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P13726\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, F3 is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of F3 can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eF3 has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of F3 can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF3\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCD antigen CD142\u003c\/strong\u003e, \u003cstrong\u003eCoagulation factor III\u003c\/strong\u003e, and \u003cstrong\u003eF 3\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952466850157,"sku":"E1195Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1195Hu.jpg?v=1769146118"},{"product_id":"human-fibrinogen-like-protein-1-fgl1-elisa-kit-bhe12104806","title":"Human Fibrinogen-like Protein 1, FGL1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibrinogen-like Protein 1 (FGL1)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q08830\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibrinogen-like Protein 1 (FGL1) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Fibrinogen-like Protein 1 (FGL1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eFibrinogen-like Protein 1 (FGL1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Fibrinogen-like Protein 1 (FGL1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibrinogen-like Protein 1 (FGL1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eFGL 1\u003c\/strong\u003e, \u003cstrong\u003eFGL1\u003c\/strong\u003e, and \u003cstrong\u003eFibrinogen-like protein 1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952500568429,"sku":"E3277Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3277Hu.jpg?v=1769146404"},{"product_id":"human-coagulation-factor-5-f5-elisa-kit-bhe12105519","title":"Human Coagulation Factor 5, F5 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF5\u003c\/strong\u003e is a molecular target commonly studied in blood coagulation research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P12259\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, F5 is frequently examined in relation to mechanistic biology studies, biomarker-focused profiling, and disease-model research. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of F5 can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eF5 has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of F5 can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF5\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eActivated protein C cofactor\u003c\/strong\u003e, \u003cstrong\u003eCoagulation factor V\u003c\/strong\u003e, and \u003cstrong\u003eCoagulation factor V heavy chain\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952520425837,"sku":"E4114hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E4114hu.jpg?v=1769146510"},{"product_id":"human-antithrombin-3-at3-elisa-kit-bhe12105661","title":"Human Antithrombin 3, AT3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAntithrombin 3 (SERPINC1)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P01008\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Antithrombin 3 (SERPINC1) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Antithrombin 3 (SERPINC1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eAntithrombin 3 (SERPINC1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Antithrombin 3 (SERPINC1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAntithrombin 3 (SERPINC1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAntithrombin-III\u003c\/strong\u003e, \u003cstrong\u003eATIII\u003c\/strong\u003e, and \u003cstrong\u003eSerpin C1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952526291309,"sku":"E4267hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E4267hu.jpg?v=1769146529"},{"product_id":"human-coagulation-factor-13-b-chain-f13b-elisa-kit-bhe12106425","title":"Human Coagulation Factor 13 B Chain, F13B ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCoagulation Factor 13 B Chain (F13B)\u003c\/strong\u003e is a molecular target commonly studied in blood coagulation research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P05160\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Coagulation Factor 13 B Chain (F13B) is frequently examined in relation to mechanistic biology studies, biomarker-focused profiling, and disease-model research. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Coagulation Factor 13 B Chain (F13B) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eCoagulation Factor 13 B Chain (F13B) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Coagulation Factor 13 B Chain (F13B) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCoagulation Factor 13 B Chain (F13B)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCoagulation factor XIII B chain\u003c\/strong\u003e, \u003cstrong\u003eF 13B\u003c\/strong\u003e, and \u003cstrong\u003eF13B\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952552046957,"sku":"E5062Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5062Hu.jpg?v=1769146634"},{"product_id":"mouse-thrombomodulin-tm-elisa-kit-bhe12108014","title":"Mouse Thrombomodulin, TM ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eThrombomodulin (THBD)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P15306\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Thrombomodulin (THBD) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Thrombomodulin (THBD) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eThrombomodulin (THBD) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Thrombomodulin (THBD) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eThrombomodulin (THBD)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCD antigen CD141\u003c\/strong\u003e, \u003cstrong\u003eFetomodulin\u003c\/strong\u003e, and \u003cstrong\u003eTHBD\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952611094893,"sku":"E0091Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0091Mo.jpg?v=1769146980"},{"product_id":"mouse-von-willebrand-factor-vwf-elisa-kit-bhe12108178","title":"Mouse Von Willebrand Factor, VWF ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVon Willebrand Factor (VWF)\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q8CIZ8\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Von Willebrand Factor (VWF) is frequently examined in relation to vascular biology and endothelial function, cardiac remodeling and injury responses, and hemostasis and thrombosis. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Von Willebrand Factor (VWF) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eVon Willebrand Factor (VWF) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Von Willebrand Factor (VWF) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVon Willebrand Factor (VWF)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003evon Willebrand antigen 2\u003c\/strong\u003e, \u003cstrong\u003evon Willebrand antigen II\u003c\/strong\u003e, and \u003cstrong\u003evon Willebrand factor\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952612143469,"sku":"E0273Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0273Mo.jpg?v=1769146992"},{"product_id":"mouse-anti-thrombin-3-at-3-elisa-kit-bhe12108577","title":"Mouse Anti-Thrombin 3, AT-3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAnti-Thrombin 3 (SERPINC1)\u003c\/strong\u003e is a molecular target commonly studied in life science research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P32261\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Anti-Thrombin 3 (SERPINC1) is frequently examined in relation to mechanistic biology studies, biomarker-focused profiling, and disease-model research. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Anti-Thrombin 3 (SERPINC1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eAnti-Thrombin 3 (SERPINC1) has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of Anti-Thrombin 3 (SERPINC1) can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAnti-Thrombin 3 (SERPINC1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAntithrombin-III\u003c\/strong\u003e, \u003cstrong\u003eATIII\u003c\/strong\u003e, and \u003cstrong\u003eSerpin C1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952614928749,"sku":"E0703Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0703Mo.jpg?v=1769147013"},{"product_id":"mouse-coagulation-factor-7-f7-elisa-kit-bhe12109327","title":"Mouse Coagulation Factor 7, F7 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF7\u003c\/strong\u003e is a molecular target commonly studied in blood coagulation research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P70375\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, F7 is frequently examined in relation to mechanistic biology studies, biomarker-focused profiling, and disease-model research. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of F7 can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eF7 has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of F7 can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF7\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCoagulation factor VII\u003c\/strong\u003e, \u003cstrong\u003eF7\u003c\/strong\u003e, and \u003cstrong\u003eFactor VII heavy chain\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952624169325,"sku":"E1470Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1470Mo.jpg?v=1769147076"},{"product_id":"mouse-coagulation-factor-3-f3-elisa-kit-bhe12109756","title":"Mouse Coagulation Factor 3, F3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF3\u003c\/strong\u003e is a molecular target commonly studied in life science research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P20352\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, F3 is frequently examined in relation to mechanistic biology studies, biomarker-focused profiling, and disease-model research. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of F3 can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. Reported regulation may involve transcriptional control as well as post-translational processes that influence stability, localization, processing, or secretion.\u003c\/p\u003e\u003ch2\u003eResearch and disease relevance\u003c\/h2\u003e\u003cp\u003eF3 has been reported as a useful readout in studies of physiological regulation and disease-associated processes. These observations make it relevant for hypothesis-driven research and biomarker exploration, while interpretation should remain grounded in the specific species, sample matrix, and study design.\u003c\/p\u003e\u003ch2\u003eInterpreting concentration measurements\u003c\/h2\u003e\u003cp\u003eMeasured levels of F3 can reflect multiple biological factors, including production rate, turnover, compartmental distribution, and sample composition. As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF3\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAA409063\u003c\/strong\u003e, \u003cstrong\u003eCD antigen CD142\u003c\/strong\u003e, and \u003cstrong\u003eCD142\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952634917229,"sku":"E1944Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1944Mo.jpg?v=1769147138"},{"product_id":"mouse-coagulation-factor-5-f5-elisa-kit-bhe12109757","title":"Mouse Coagulation Factor 5, F5 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF5\u003c\/strong\u003e is a molecular target commonly studied in cardiovascular research. 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As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF5\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eActivated protein C cofactor\u003c\/strong\u003e, \u003cstrong\u003eAI173222\u003c\/strong\u003e, and \u003cstrong\u003eCf5\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952634982765,"sku":"E1945Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1945Mo.jpg?v=1769147138"},{"product_id":"mouse-coagulation-factor-8-f8-elisa-kit-bhe12109758","title":"Mouse Coagulation Factor 8, F8 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF8\u003c\/strong\u003e is a molecular target commonly studied in immunology research. 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This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P79335\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Plasminogen Activator Inhibitor 1 (SERPINE1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Plasminogen Activator Inhibitor 1 (SERPINE1) can vary across tissues and cell types and may change under conditions such as immune activation, stress responses, injury, infection, or metabolic perturbation. 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As a result, conclusions are often supported by considering broader pathway context and complementary readouts rather than relying on a single analyte alone.\u003c\/p\u003e\u003ch2\u003eNomenclature\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eF10\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eActivated factor Xa heavy chain\u003c\/strong\u003e, \u003cstrong\u003eCoagulation factor X\u003c\/strong\u003e, and \u003cstrong\u003eF1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952672698733,"sku":"E0490Ra-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0490Ra.jpg?v=1769147373"}],"url":"https:\/\/www.ebiohippo.com\/collections\/rs-fibrinogen-d-dimer-thrombin.oembed?page=3","provider":"BioHippo","version":"1.0","type":"link"}