{"title":"Collagen \/ Laminin \/ Fibronectin","description":null,"products":[{"product_id":"human-fibronectin-elisa-kit-ez-set-diy-antibody-pairs-bhe21000047","title":"Human Fibronectin ELISA Kit EZ-Set™ (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Cold-insoluble globulin, CIG, Anastellin, Ugl-Y1, Ugl-Y2, Ugl-Y3.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFN1\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\u003eEndocrinology \u0026amp; Hormones\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":52920802738541,"sku":"EZ0349","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0349.png?v=1769077485"},{"product_id":"rat-laminin-elisa-kit-ez-set-diy-antibody-pairs-bhe21000048","title":"Rat Laminin ELISA Kit EZ-Set™ (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Laminin subunit beta-2, Laminin chain B3, Laminin-11 subunit beta, Laminin-14 subunit beta, Laminin-15 subunit beta, Laminin-3 subunit beta, Laminin-4 subunit beta, Laminin-7 subunit beta.\u003c\/p\u003e\u003cp\u003eRat \u003cstrong\u003eLaminin\u003c\/strong\u003e (\u003cstrong\u003eLaminin\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":52920802771309,"sku":"EZ0435","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0435_23fc789f-d881-407c-8205-e2f92352016f.png?v=1769077485"},{"product_id":"mouse-laminin-elisa-kit-ez-set-diy-antibody-pairs-bhe21000049","title":"Mouse Laminin ELISA Kit EZ-Set™ (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Laminin subunit alpha-3, Epiligrin subunit alpha, Kalinin subunit alpha, Laminin-5 subunit alpha, Laminin-6 subunit alpha, Laminin-7 subunit alpha, Nicein subunit alpha, Lama3.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eLaminin\u003c\/strong\u003e (\u003cstrong\u003eLaminin\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":"5 plates\/kit","offer_id":52920802804077,"sku":"EZ0436","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/EZ0436-mouse-lama1-ez-set-elisa-kit-diy-antibody-pairs.jpg?v=1769077485"},{"product_id":"human-laminin-elisa-kit-ez-set-diy-antibody-pairs-bhe21000061","title":"Human Laminin ELISA Kit EZ-Set™ (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Laminin subunit alpha-3, Epiligrin 170 kDa subunit, E170, Epiligrin subunit alpha, Kalinin subunit alpha, Laminin-5 subunit alpha, Laminin-6 subunit alpha, Laminin-7 subunit alpha.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eLaminin\u003c\/strong\u003e (\u003cstrong\u003eLaminin\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\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":52920803197293,"sku":"EZ0434","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0434.png?v=1769077490"},{"product_id":"mouse-fibronectin-picokine-quick-elisa-kit-bhe21000172","title":"Mouse Fibronectin PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Anastellin, Fn1.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFn1\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":"96 wells\/kit, with removable strips.","offer_id":52920806900077,"sku":"FEK0351","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/fek0351_2c4bb777-28a3-4aa4-ba48-b265d8f04d14.png?v=1769077536"},{"product_id":"rat-fibronectin-picokine-quick-elisa-kit-bhe21000173","title":"Rat Fibronectin PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Anastellin, Fn1.\u003c\/p\u003e\u003cp\u003eRat \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFn1\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\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":"96 wells\/kit, with removable strips.","offer_id":52920806932845,"sku":"FEK0350","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0350.png?v=1769077536"},{"product_id":"human-laminin-picokine-quick-elisa-kit-bhe21000241","title":"Human Laminin PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003eHuman \u003cstrong\u003eLaminin\u003c\/strong\u003e (\u003cstrong\u003eCST3\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":52920809357677,"sku":"FEK0434","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/fek0434_18a62625-7b2e-452d-bdca-676123e17b0d.png?v=1769077568"},{"product_id":"mouse-endostatin-picokine-quick-elisa-kit-bhe21000335","title":"Mouse Endostatin PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003eMouse \u003cstrong\u003eEndostatin\u003c\/strong\u003e (\u003cstrong\u003eCol18a1\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\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":52920812568941,"sku":"FEK1376","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/fek1376.png?v=1769077627"},{"product_id":"rat-endostatin-picokine-quick-elisa-kit-bhe21000336","title":"Rat Endostatin PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003eRat \u003cstrong\u003eEndostatin\u003c\/strong\u003e (\u003cstrong\u003eCol18a1\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\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":52920812601709,"sku":"FEK1377","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/fek1377_1.png?v=1769077628"},{"product_id":"human-fibronectin-elisa-kit-picokine-bhe21000364","title":"Human Fibronectin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Cold-insoluble globulin, CIG, Anastellin, Ugl-Y1, Ugl-Y2, Ugl-Y3.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFN1\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":52920813519213,"sku":"EK0349","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0349_4c5fb403-8184-4614-9639-53e2c3880bd9.png?v=1769077645"},{"product_id":"rat-fibronectin-elisa-kit-picokine-bhe21000365","title":"Rat Fibronectin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Anastellin, Fn1.\u003c\/p\u003e\u003cp\u003eRat \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFN1\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. 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":52920813551981,"sku":"EK0350","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0350_1.png?v=1769077646"},{"product_id":"mouse-fibronectin-elisa-kit-picokine-bhe21000366","title":"Mouse Fibronectin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Anastellin, Fn1.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFN1\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. 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":52920813584749,"sku":"EK0351","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0351_2_d478b2d2-2a3e-4287-b26a-747d73f2d04c.png?v=1769077646"},{"product_id":"human-laminin-elisa-kit-picokine-bhe21000432","title":"Human Laminin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Laminin subunit alpha-1, Laminin A chain, Laminin-1 subunit alpha, Laminin-3 subunit alpha, S-laminin subunit alpha, Laminin subunit beta-1, Laminin B1 chain, Laminin subunit gamma-1.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eLaminin\u003c\/strong\u003e (\u003cstrong\u003eLAMA1\/LAMB1\/LAMC1\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":52920816206189,"sku":"EK0434","price":450.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0434_1.png?v=1769077683"},{"product_id":"rat-laminin-elisa-kit-picokine-bhe21000433","title":"Rat Laminin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Laminin subunit beta-2, Laminin chain B3, Laminin-11 subunit beta, Laminin-14 subunit beta, Laminin-15 subunit beta, Laminin-3 subunit beta, Laminin-4 subunit beta, Laminin-7 subunit beta.\u003c\/p\u003e\u003cp\u003eRat \u003cstrong\u003eLaminin\u003c\/strong\u003e (\u003cstrong\u003eLAMA1; LAMA2; LAMB1; LAMB2\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":"96 wells\/kit, with removable strips.","offer_id":52920816238957,"sku":"EK0435","price":750.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0435.png?v=1769077684"},{"product_id":"mouse-laminin-elisa-kit-picokine-bhe21000434","title":"Mouse Laminin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Laminin subunit alpha-3, Epiligrin subunit alpha, Kalinin subunit alpha, Laminin-5 subunit alpha, Laminin-6 subunit alpha, Laminin-7 subunit alpha, Nicein subunit alpha, Lama3.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eLaminin\u003c\/strong\u003e (\u003cstrong\u003eLAMA1; LAMA2; LAMB1; LAMB2\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":"96 wells\/kit, with removable strips.","offer_id":52920816271725,"sku":"EK0436","price":750.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0436_2.png?v=1769077684"},{"product_id":"human-endostatin-elisa-kit-picokine-bhe21000678","title":"Human Endostatin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Collagen alpha-1 (XVIII) chain, Endostatin, COL18A1.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eEndostatin\u003c\/strong\u003e (\u003cstrong\u003eCOL18A1\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":52920824529261,"sku":"EK0886","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0886.png?v=1769077799"},{"product_id":"human-periostin-osf2-elisa-kit-picokine-bhe21000748","title":"Human Periostin\/OSF2 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Periostin, PN, Osteoblast-specific factor 2, OSF-2, POSTN, OSF2.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePeriostin\/OSF2\u003c\/strong\u003e (\u003cstrong\u003ePOSTN\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":52920827773293,"sku":"EK0985","price":399.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek0985_3.png?v=1769077830"},{"product_id":"mouse-periostin-osf2-elisa-kit-picokine-bhe21000807","title":"Mouse Periostin\/OSF2 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Periostin, PN, Osteoblast-specific factor 2, OSF-2, Postn, Osf2.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003ePeriostin\/OSF2\u003c\/strong\u003e (\u003cstrong\u003ePOSTN\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":52920831115629,"sku":"EK1187","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1187.jpg?v=1769077864"},{"product_id":"mouse-endostatin-elisa-kit-picokine-bhe21000965","title":"Mouse Endostatin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Collagen alpha-1 (XVIII) chain, Endostatin, Col18a1.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eEndostatin\u003c\/strong\u003e (\u003cstrong\u003eCOL18A1\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\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":"96 wells\/kit, with removable strips.","offer_id":52920836686189,"sku":"EK1376","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1376.png?v=1769077956"},{"product_id":"human-tenascin-c-tnc-elisa-kit-picokine-bhe21000987","title":"Human Tenascin-C\/TNC ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tenascin, TN, Cytotactin, GMEM, GP 150-225, Glioma-associated-extracellular matrix antigen, Hexabrachion, JI.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eTenascin-C\/TNC\u003c\/strong\u003e (\u003cstrong\u003eTNC\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":52920839438701,"sku":"EK1170","price":450.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1170.jpg?v=1769077972"},{"product_id":"rat-endostatin-elisa-kit-picokine-bhe21001132","title":"Rat Endostatin ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Collagen type XVIII, alpha (I) chain, Col18a1.\u003c\/p\u003e\u003cp\u003eRat \u003cstrong\u003eEndostatin\u003c\/strong\u003e (\u003cstrong\u003eCol18a1\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":52920854479213,"sku":"EK1377","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1377_1.png?v=1769078054"},{"product_id":"human-pro-collagen-i-alpha-1-col1a1-elisa-kit-picokine-bhe21001357","title":"Human Pro-collagen I alpha 1\/COL1A1 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Collagen alpha-1 (I) chain, Alpha-1 type I collagen, COL1A1.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003ePro-collagen I alpha 1\/COL1A1\u003c\/strong\u003e (\u003cstrong\u003eCOL1A1\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":52920872468845,"sku":"EK1692","price":450.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1692_1.png?v=1769078173"},{"product_id":"human-tenascin-r-elisa-kit-picokine-bhe21001515","title":"Human Tenascin-R ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Tenascin-R, TN-R, Janusin, Restrictin, TNR.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eTenascin-R\u003c\/strong\u003e (\u003cstrong\u003eTNR\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":52920879022445,"sku":"EK1931","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek1931_90ff91f7-cceb-478a-b50f-3fd1319e6546.png?v=1769078266"},{"product_id":"human-ctgf-elisa-kit-picokine-bhe21001694","title":"Human CTGF ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003eHuman \u003cstrong\u003eCTGF\u003c\/strong\u003e (\u003cstrong\u003eCCN2\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. Growth factors and morphogens regulate cell proliferation, differentiation, survival, and tissue remodeling by engaging surface receptors and activating downstream signaling cascades. Their activity is often context-dependent, shaped by receptor availability, extracellular matrix binding, and feedback regulation.\u003c\/p\u003e\u003ch2\u003eBiological function and mechanism\u003c\/h2\u003e\u003cp\u003eIn many systems, growth-factor signaling integrates environmental cues with developmental or repair programs. Downstream pathways frequently include kinase signaling modules and transcriptional responses that alter cell-cycle control, migration, or lineage specification. Because these signals can be transient, quantitative measurements are useful for understanding timing and dose dependence.\u003c\/p\u003e\u003ch2\u003eWhy it matters in research\u003c\/h2\u003e\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003ePathway engagement:\u003c\/strong\u003e Concentration changes can indicate activation of growth, survival, or differentiation programs.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eTissue remodeling:\u003c\/strong\u003e Levels may relate to repair, fibrosis, angiogenesis, or developmental patterning in model systems.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMechanistic studies:\u003c\/strong\u003e Tracking abundance alongside downstream markers helps connect ligand availability to signaling output.\u003c\/li\u003e\n\u003c\/ul\u003e\u003ch2\u003eDisease and translational relevance\u003c\/h2\u003e\u003cp\u003eAltered growth-factor signaling has been reported across diverse conditions, including cancer biology, cardiovascular remodeling, wound repair, and metabolic dysfunction. For research interpretation, consider whether the measured form represents active ligand, bound complexes, or processed fragments, as these can influence apparent levels.\u003c\/p\u003e","brand":"Boster Bio","offers":[{"title":"96 wells\/kit, with removable strips.","offer_id":52920893473133,"sku":"EK2149","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek2149.png?v=1769078351"},{"product_id":"human-fibronectin-picokine-quick-elisa-kit-bhe21001903","title":"Human Fibronectin PicoKine® Quick ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Cold-insoluble globulin, CIG, Anastellin, Ugl-Y1, Ugl-Y2, Ugl-Y3.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFN1\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":52920904483181,"sku":"FEK0349","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/fek0349_1_55d9ac08-e3d2-4af7-b3fd-c9e11ee2f11d.png?v=1769078455"},{"product_id":"human-col2a1-elisa-kit-picokine-bhe21001926","title":"Human COL2A1 ELISA Kit PicoKine®","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Collagen alpha-1 (II) chain, Alpha-1 type II collagen, Chondrocalcin.\u003c\/p\u003e\u003cp\u003eHuman \u003cstrong\u003eCOL2A1\u003c\/strong\u003e (\u003cstrong\u003eCOL2A1\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":"96 wells\/kit, with removable strips.","offer_id":52920905236845,"sku":"EK2307","price":499.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ek2307.jpg?v=1769078466"},{"product_id":"rat-fibronectin-ez-set-and-trade-elisa-kit-diy-antibody-pairs-bhe21002014","title":"Rat Fibronectin EZ-Set\u0026trade; ELISA Kit (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Anastellin, Fn1.\u003c\/p\u003e\u003cp\u003eRat \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFN1\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":"5 plates\/kit","offer_id":52920908611949,"sku":"EZ0350","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0350.png?v=1769078515"},{"product_id":"mouse-fibronectin-ez-set-and-trade-elisa-kit-diy-antibody-pairs-bhe21002015","title":"Mouse Fibronectin EZ-Set\u0026trade; ELISA Kit (DIY Antibody Pairs)","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAlso known as:\u003c\/strong\u003e Fibronectin, FN, Anastellin, Fn1.\u003c\/p\u003e\u003cp\u003eMouse \u003cstrong\u003eFibronectin\u003c\/strong\u003e (\u003cstrong\u003eFN1\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\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":"5 plates\/kit","offer_id":52920908644717,"sku":"EZ0351","price":500.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/ez0351.png?v=1769078516"},{"product_id":"bovine-fibronectin-fn-elisa-kit-bhe12100397","title":"Bovine Fibronectin, FN ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin (FN)\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: P07589\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin (FN) 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 Fibronectin (FN) 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\u003eFibronectin (FN) 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 Fibronectin (FN) 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\u003eFibronectin (FN)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAnastellin]\u003c\/strong\u003e, \u003cstrong\u003eFibronectin\u003c\/strong\u003e, and \u003cstrong\u003eFN\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":52952447353197,"sku":"E2016Bo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2016Bo.jpg?v=1769145935"},{"product_id":"canine-fibronectin-fn-elisa-kit-bhe12100659","title":"Canine Fibronectin, FN ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin (FN)\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: Q28275\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin (FN) 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 Fibronectin (FN) 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\u003eFibronectin (FN) 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 Fibronectin (FN) 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\u003eFibronectin (FN)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eFibronectin\u003c\/strong\u003e, \u003cstrong\u003eFN\u003c\/strong\u003e, and \u003cstrong\u003eFragment\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":52952450302317,"sku":"E0116Ca-96T","price":475.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0116Ca.jpg?v=1769145963"},{"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":"horse-fibronectin-fn1-elisa-kit-bhe12101726","title":"Horse Fibronectin, FN1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eHorse Fibronectin (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: Q28377\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Horse Fibronectin (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 Horse Fibronectin (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\u003eHorse Fibronectin (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 Horse Fibronectin (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\u003eHorse Fibronectin (FN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAnastellin\u003c\/strong\u003e, \u003cstrong\u003eFibronectin\u003c\/strong\u003e, and \u003cstrong\u003eFN\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":52952454037869,"sku":"E0118HO-96T","price":498.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0118HO.jpg?v=1769145992"},{"product_id":"human-vitronectin-vtn-elisa-kit-bhe12101995","title":"Human Vitronectin, VTN ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVitronectin (VTN)\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: P04004\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Vitronectin (VTN) 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 Vitronectin (VTN) 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\u003eVitronectin (VTN) 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 Vitronectin (VTN) 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\u003eVitronectin (VTN)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eSerum-spreading factor\u003c\/strong\u003e, \u003cstrong\u003eSomatomedin-B]\u003c\/strong\u003e, and \u003cstrong\u003eS-protein\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":52952458264941,"sku":"E0284Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0284Hu.jpg?v=1769146036"},{"product_id":"human-tenascin-r-tn-r-elisa-kit-bhe12103092","title":"Human Tenascin-R, TN-R ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTenascin-R (TN-R)\u003c\/strong\u003e is a molecular target commonly studied in neuroscience 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: Q92752\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Tenascin-R (TN-R) is frequently examined in relation to neuronal signaling and synaptic function, neuroinflammation and glial responses, and neurodegeneration models. 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 Tenascin-R (TN-R) 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\u003eTenascin-R (TN-R) 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 Tenascin-R (TN-R) 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\u003eTenascin-R (TN-R)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eJanusin\u003c\/strong\u003e, \u003cstrong\u003eRestrictin\u003c\/strong\u003e, and \u003cstrong\u003eTenascin-R\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":52952468816237,"sku":"E1475Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1475Hu.jpg?v=1769146133"},{"product_id":"human-fibronectin-fn-elisa-kit-bhe12103563","title":"Human Fibronectin, FN ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin (FN1)\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: P02751\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin (FN1) 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 Fibronectin (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\u003eFibronectin (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 Fibronectin (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\u003eFibronectin (FN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAnastellin\u003c\/strong\u003e, \u003cstrong\u003eCIG\u003c\/strong\u003e, and \u003cstrong\u003eCold-insoluble globulin\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":52952474354029,"sku":"E2002Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2002Hu.jpg?v=1769146171"},{"product_id":"human-fibronectin-type-3-domain-containing-protein-5-fndc5-elisa-kit-bhe12104735","title":"Human Fibronectin Type 3 Domain-containing Protein 5, FNDC5 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin Type 3 Domain-containing Protein 5 (FNDC5)\u003c\/strong\u003e is a molecular target commonly studied in metabolism 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: Q8NAU1\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin Type 3 Domain-containing Protein 5 (FNDC5) is frequently examined in relation to energy homeostasis, glucose and lipid metabolism, and insulin sensitivity and endocrine regulation. 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 Fibronectin Type 3 Domain-containing Protein 5 (FNDC5) 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\u003eFibronectin Type 3 Domain-containing Protein 5 (FNDC5) 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 Fibronectin Type 3 Domain-containing Protein 5 (FNDC5) 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\u003eFibronectin Type 3 Domain-containing Protein 5 (FNDC5)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eFibronectin type III domain-containing protein 5\u003c\/strong\u003e, \u003cstrong\u003eFibronectin type III repeat-containing protein 2\u003c\/strong\u003e, and \u003cstrong\u003eFNDC 5\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":52952498962797,"sku":"E3206Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3206Hu.jpg?v=1769146387"},{"product_id":"human-periostin-postn-elisa-kit-bhe12104755","title":"Human Periostin, POSTN ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003ePeriostin (POSTN)\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: Q15063\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Periostin (POSTN) 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 Periostin (POSTN) 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\u003ePeriostin (POSTN) 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 Periostin (POSTN) 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\u003ePeriostin (POSTN)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eOSF-2\u003c\/strong\u003e, \u003cstrong\u003eOsteoblast-specific factor 2\u003c\/strong\u003e, and \u003cstrong\u003ePeriostin\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":52952499388781,"sku":"E3226Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3226Hu.jpg?v=1769146390"},{"product_id":"human-tenascin-n-tnn-elisa-kit-bhe12105019","title":"Human Tenascin-N, TNN ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eTenascin-N (TNN)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction 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: Q9UQP3\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Tenascin-N (TNN) 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 Tenascin-N (TNN) 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\u003eTenascin-N (TNN) 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 Tenascin-N (TNN) 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\u003eTenascin-N (TNN)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eTenascin-N\u003c\/strong\u003e, \u003cstrong\u003eTenascin-W\u003c\/strong\u003e, and \u003cstrong\u003eTNN\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":52952505450861,"sku":"E3528Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3528Hu.jpg?v=1769146444"},{"product_id":"human-laminin-subunit-alpha-1-lama1-elisa-kit-bhe12106042","title":"Human Laminin Subunit Alpha-1, LAMA1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLaminin Subunit Alpha-1 (LAMA1)\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: P25391\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Laminin Subunit Alpha-1 (LAMA1) 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 Laminin Subunit Alpha-1 (LAMA1) 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\u003eLaminin Subunit Alpha-1 (LAMA1) 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 Laminin Subunit Alpha-1 (LAMA1) 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\u003eLaminin Subunit Alpha-1 (LAMA1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eLAMA 1\u003c\/strong\u003e, \u003cstrong\u003eLAMA1\u003c\/strong\u003e, and \u003cstrong\u003eLaminin A 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":52952536056173,"sku":"E4755Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}]},{"product_id":"human-collagen-triple-helix-repeat-containing-protein-1-cthrc1-elisa-kit-bhe12106444","title":"Human Collagen Triple Helix Repeat-containing Protein 1, CTHRC1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCollagen Triple Helix Repeat-containing Protein 1 (CTHRC1)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction 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: Q96CG8\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Collagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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 Collagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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\u003eCollagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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 Collagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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\u003eCollagen Triple Helix Repeat-containing Protein 1 (CTHRC1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCollagen triple helix repeat-containing protein 1\u003c\/strong\u003e and \u003cstrong\u003eCTHRC1\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":52952552178029,"sku":"E5081Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5081Hu.jpg?v=1769146635"},{"product_id":"human-fibronectin-type-3-and-spry-domain-containing-protein-1-fsd1-elisa-kit-bhe12106657","title":"Human Fibronectin Type 3 and Spry Domain-containing Protein 1, FSD1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin Type 3 and Spry Domain-containing Protein 1 (FSD1)\u003c\/strong\u003e is a molecular target commonly studied in epigenetics and nuclear signaling 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: Q9BTV5\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin Type 3 and Spry Domain-containing Protein 1 (FSD1) 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 Fibronectin Type 3 and Spry Domain-containing Protein 1 (FSD1) 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\u003eFibronectin Type 3 and Spry Domain-containing Protein 1 (FSD1) 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 Fibronectin Type 3 and Spry Domain-containing Protein 1 (FSD1) 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\u003eFibronectin Type 3 and Spry Domain-containing Protein 1 (FSD1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eFibronectin type III and SPRY domain-containing protein 1\u003c\/strong\u003e, \u003cstrong\u003eFSD1\u003c\/strong\u003e, and \u003cstrong\u003eGLFND\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":52952566333805,"sku":"E5294Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5294Hu.jpg?v=1769146701"},{"product_id":"human-fibronectin-type-iii-domain-containing-protein-3b-fndc3b-elisa-kit-bhe12106658","title":"Human Fibronectin Type Iii Domain-containing Protein 3B, FNDC3B ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin Type Iii Domain-containing Protein 3B (FNDC3B)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction 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: Q53EP0\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin Type Iii Domain-containing Protein 3B (FNDC3B) 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 Fibronectin Type Iii Domain-containing Protein 3B (FNDC3B) 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\u003eFibronectin Type Iii Domain-containing Protein 3B (FNDC3B) 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 Fibronectin Type Iii Domain-containing Protein 3B (FNDC3B) 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\u003eFibronectin Type Iii Domain-containing Protein 3B (FNDC3B)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eFactor for adipocyte differentiation 104\u003c\/strong\u003e, \u003cstrong\u003eFAD104\u003c\/strong\u003e, and \u003cstrong\u003eFibronectin type III domain-containing protein 3B\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":52952567021933,"sku":"E5295Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5295Hu.jpg?v=1769146702"},{"product_id":"human-laminin-subunit-alpha-3-lama3-elisa-kit-bhe12106913","title":"Human Laminin Subunit Alpha-3, LAMA3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLaminin Subunit Alpha-3 (LAMA3)\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: Q16787\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Laminin Subunit Alpha-3 (LAMA3) 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 Laminin Subunit Alpha-3 (LAMA3) 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\u003eLaminin Subunit Alpha-3 (LAMA3) 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 Laminin Subunit Alpha-3 (LAMA3) 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\u003eLaminin Subunit Alpha-3 (LAMA3)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE170\u003c\/strong\u003e, \u003cstrong\u003eEpiligrin 170 kDa subunit\u003c\/strong\u003e, and \u003cstrong\u003eEpiligrin subunit alpha\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":52952582259053,"sku":"E5551Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5551Hu.jpg?v=1769146788"},{"product_id":"human-laminin-subunit-alpha-4-lama4-elisa-kit-bhe12106914","title":"Human Laminin Subunit Alpha-4, LAMA4 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLaminin Subunit Alpha-4 (LAMA4)\u003c\/strong\u003e is a molecular target commonly studied in neuroscience 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: Q16363\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Laminin Subunit Alpha-4 (LAMA4) is frequently examined in relation to neuronal signaling and synaptic function, neuroinflammation and glial responses, and neurodegeneration models. 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 Laminin Subunit Alpha-4 (LAMA4) 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\u003eLaminin Subunit Alpha-4 (LAMA4) 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 Laminin Subunit Alpha-4 (LAMA4) 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\u003eLaminin Subunit Alpha-4 (LAMA4)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eLAMA 4\u003c\/strong\u003e, \u003cstrong\u003eLAMA4\u003c\/strong\u003e, and \u003cstrong\u003eLaminin subunit alpha-4\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":52952582291821,"sku":"E5552Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5552Hu.jpg?v=1769146788"},{"product_id":"human-laminin-subunit-gamma-1-lamc1-elisa-kit-bhe12106915","title":"Human Laminin Subunit Gamma-1, LAMC1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLaminin Subunit Gamma-1 (LAMC1)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction 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: P11047\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Laminin Subunit Gamma-1 (LAMC1) 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 Laminin Subunit Gamma-1 (LAMC1) 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\u003eLaminin Subunit Gamma-1 (LAMC1) 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 Laminin Subunit Gamma-1 (LAMC1) 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\u003eLaminin Subunit Gamma-1 (LAMC1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eLAMC 1\u003c\/strong\u003e, \u003cstrong\u003eLAMC1\u003c\/strong\u003e, and \u003cstrong\u003eLaminin B2 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":52952582357357,"sku":"E5553Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5553Hu.jpg?v=1769146789"},{"product_id":"human-laminin-1-ln-b1-elisa-kit-bhe12106916","title":"Human Laminin ?1, LN-B1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eLaminin Β1 (LMNB1)\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: P20700\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Laminin Β1 (LMNB1) 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 Laminin Β1 (LMNB1) 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\u003eLaminin Β1 (LMNB1) 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 Laminin Β1 (LMNB1) 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\u003eLaminin Β1 (LMNB1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eLamin-B1\u003c\/strong\u003e, \u003cstrong\u003eLMNB 1\u003c\/strong\u003e, and \u003cstrong\u003eLMNB1\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":52952582390125,"sku":"E5554Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5554Hu.jpg?v=1769146789"},{"product_id":"mouse-fibronectin-fn-elisa-kit-bhe12108001","title":"Mouse Fibronectin, FN ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin (FN1)\u003c\/strong\u003e is a molecular target commonly studied in 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: P11276\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin (FN1) is frequently examined in relation to innate and adaptive immune responses, cytokine signaling networks, and immune cell activation and trafficking. 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 Fibronectin (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\u003eFibronectin (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 Fibronectin (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\u003eFibronectin (FN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAnastellin\u003c\/strong\u003e, \u003cstrong\u003eFibronectin\u003c\/strong\u003e, and \u003cstrong\u003eFN\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":52952610865517,"sku":"E0077Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0077Mo.jpg?v=1769146979"},{"product_id":"mouse-fibronectin-type-3-domain-containing-protein-5-fndc5-elisa-kit-bhe12109143","title":"Mouse Fibronectin Type 3 Domain-containing Protein 5, FNDC5 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eFibronectin Type 3 Domain-containing Protein 5 (FNDC5)\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: Q8K4Z2\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Fibronectin Type 3 Domain-containing Protein 5 (FNDC5) 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 Fibronectin Type 3 Domain-containing Protein 5 (FNDC5) 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\u003eFibronectin Type 3 Domain-containing Protein 5 (FNDC5) 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 Fibronectin Type 3 Domain-containing Protein 5 (FNDC5) 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\u003eFibronectin Type 3 Domain-containing Protein 5 (FNDC5)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e1500001L03Rik\u003c\/strong\u003e, \u003cstrong\u003eAI836596\u003c\/strong\u003e, and \u003cstrong\u003eC87088\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":52952620466541,"sku":"E1278Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1278Mo.jpg?v=1769147060"},{"product_id":"mouse-vitronectin-vnr-elisa-kit-bhe12109272","title":"Mouse Vitronectin, VNR ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eVitronectin (VTN)\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: P29788\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Vitronectin (VTN) 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 Vitronectin (VTN) 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\u003eVitronectin (VTN) 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 Vitronectin (VTN) 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\u003eVitronectin (VTN)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eSerum-spreading factor\u003c\/strong\u003e, \u003cstrong\u003eS-protein\u003c\/strong\u003e, and \u003cstrong\u003eVitronectin\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":52952623055213,"sku":"E1409Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1409Mo.jpg?v=1769147069"},{"product_id":"mouse-collagen-triple-helix-repeat-containing-protein-1-cthrc1-elisa-kit-bhe12109772","title":"Mouse Collagen Triple Helix Repeat-containing Protein 1, CTHRC1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eCollagen Triple Helix Repeat-containing Protein 1 (CTHRC1)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction 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: Q9D1D6\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Collagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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 Collagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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\u003eCollagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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 Collagen Triple Helix Repeat-containing Protein 1 (CTHRC1) 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\u003eCollagen Triple Helix Repeat-containing Protein 1 (CTHRC1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e1110014B07Rik\u003c\/strong\u003e, \u003cstrong\u003eCollagen triple helix repeat-containing protein 1\u003c\/strong\u003e, and \u003cstrong\u003eCTHRC1\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":52952635244909,"sku":"E1960Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1960Mo.jpg?v=1769147139"}],"url":"https:\/\/www.ebiohippo.com\/collections\/rs-collagen-laminin-fibronectin.oembed?page=5","provider":"BioHippo","version":"1.0","type":"link"}