{"title":"Ubiquitin-Proteasome System","description":null,"products":[{"product_id":"bovine-ubiquitin-like-protein-isg15-isg15-elisa-kit-bhe12100331","title":"Bovine Ubiquitin-like Protein Isg15, ISG15 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-like Protein Isg15 (ISG15)\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: O02741\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-like Protein Isg15 (ISG15) 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 Ubiquitin-like Protein Isg15 (ISG15) 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\u003eUbiquitin-like Protein Isg15 (ISG15) 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 Ubiquitin-like Protein Isg15 (ISG15) 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\u003eUbiquitin-like Protein Isg15 (ISG15)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eBoUCRP\u003c\/strong\u003e, \u003cstrong\u003eInterferon-stimulated gene product 17\u003c\/strong\u003e, and \u003cstrong\u003eISG15\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":52952446959981,"sku":"E0359Bo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0359Bo.jpg?v=1769145932"},{"product_id":"human-beclin-1-becn1-elisa-kit-bhe12103571","title":"Human Beclin-1, BECN1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBeclin-1 (BECN1)\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: Q14457\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Beclin-1 (BECN1) 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 Beclin-1 (BECN1) 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\u003eBeclin-1 (BECN1) 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 Beclin-1 (BECN1) 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\u003eBeclin-1 (BECN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eBeclin-1\u003c\/strong\u003e, \u003cstrong\u003eBeclin-1-C 35 kDa\u003c\/strong\u003e, and \u003cstrong\u003eBeclin-1-C 37 kDa\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":52952474452333,"sku":"E2011Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2011Hu.jpg?v=1769146171"},{"product_id":"human-ubiquitin-carboxyl-terminalhydrolase-l1-uchl1-elisa-kit-bhe12103866","title":"Human Ubiquitin Carboxyl Terminalhydrolase L1, UCHL1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin Carboxyl Terminalhydrolase L1 (USP1)\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: O94782\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin Carboxyl Terminalhydrolase L1 (USP1) 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 Ubiquitin Carboxyl Terminalhydrolase L1 (USP1) 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\u003eUbiquitin Carboxyl Terminalhydrolase L1 (USP1) 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 Ubiquitin Carboxyl Terminalhydrolase L1 (USP1) 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\u003eUbiquitin Carboxyl Terminalhydrolase L1 (USP1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eDeubiquitinating enzyme 1\u003c\/strong\u003e, \u003cstrong\u003ehUBP\u003c\/strong\u003e, and \u003cstrong\u003eUbiquitin carboxyl-terminal hydrolase 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":52952479564141,"sku":"E2328Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2328Hu.jpg?v=1769146214"},{"product_id":"human-ubiquitin-specific-peptidase-8-usp8-elisa-kit-bhe12103876","title":"Human Ubiquitin Specific Peptidase 8, USP8 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin Specific Peptidase 8 (USP8)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q96LD8\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin Specific Peptidase 8 (USP8) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Ubiquitin Specific Peptidase 8 (USP8) 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\u003eUbiquitin Specific Peptidase 8 (USP8) 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 Ubiquitin Specific Peptidase 8 (USP8) 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\u003eUbiquitin Specific Peptidase 8 (USP8)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eDEN1\u003c\/strong\u003e, \u003cstrong\u003eDeneddylase-1\u003c\/strong\u003e, and \u003cstrong\u003eNEDD8-specific protease 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":52952479924589,"sku":"E2338Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2338Hu.jpg?v=1769146217"},{"product_id":"human-proteasome-subunit-beta-type-6-psmb6-elisa-kit-bhe12103965","title":"Human Proteasome Subunit Beta Type 6, PSMB6 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eProteasome Subunit Beta Type 6 (PSMB6)\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: P28072\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Proteasome Subunit Beta Type 6 (PSMB6) 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 Proteasome Subunit Beta Type 6 (PSMB6) 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\u003eProteasome Subunit Beta Type 6 (PSMB6) 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 Proteasome Subunit Beta Type 6 (PSMB6) 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\u003eProteasome Subunit Beta Type 6 (PSMB6)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eMacropain delta chain\u003c\/strong\u003e, \u003cstrong\u003eMulticatalytic endopeptidase complex delta chain\u003c\/strong\u003e, and \u003cstrong\u003eProteasome delta 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":52952482251117,"sku":"E2427Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2427Hu.jpg?v=1769146235"},{"product_id":"human-e3-ubiquitin-protein-ligase-rnf167-rnf167-elisa-kit-bhe12104976","title":"Human E3 Ubiquitin Protein Ligase Rnf167, RNF167 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin Protein Ligase Rnf167 (RNF167)\u003c\/strong\u003e is a molecular target commonly studied in life science research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q9H6Y7\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin Protein Ligase Rnf167 (RNF167) 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 E3 Ubiquitin Protein Ligase Rnf167 (RNF167) 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\u003eE3 Ubiquitin Protein Ligase Rnf167 (RNF167) 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 E3 Ubiquitin Protein Ligase Rnf167 (RNF167) 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\u003eE3 Ubiquitin Protein Ligase Rnf167 (RNF167)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase RNF167\u003c\/strong\u003e, \u003cstrong\u003eRING finger protein 167\u003c\/strong\u003e, and \u003cstrong\u003eRING105\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":52952504631661,"sku":"E3470Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3470Hu.jpg?v=1769146436"},{"product_id":"human-ubiquitin-carboxyl-terminalhydrolase-bap1-bap1-elisa-kit-bhe12105358","title":"Human Ubiquitin Carboxyl Terminalhydrolase Bap1, BAP1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin Carboxyl Terminalhydrolase Bap1 (BAP1)\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: Q92560\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin Carboxyl Terminalhydrolase Bap1 (BAP1) 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 Ubiquitin Carboxyl Terminalhydrolase Bap1 (BAP1) 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\u003eUbiquitin Carboxyl Terminalhydrolase Bap1 (BAP1) 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 Ubiquitin Carboxyl Terminalhydrolase Bap1 (BAP1) 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\u003eUbiquitin Carboxyl Terminalhydrolase Bap1 (BAP1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eBAP1\u003c\/strong\u003e, \u003cstrong\u003eBRCA1-associated protein 1\u003c\/strong\u003e, and \u003cstrong\u003eCerebral protein 6\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952513642861,"sku":"E3920Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3920Hu.jpg?v=1769146492"},{"product_id":"human-e3-sumo-protein-ligase-egr2-egr2-elisa-kit-bhe12105363","title":"Human E3 Sumo-protein Ligase Egr2, EGR2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eEgr2\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: P11161\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Egr2 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 Egr2 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\u003eEgr2 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 Egr2 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\u003eEgr2\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAT591\u003c\/strong\u003e, \u003cstrong\u003eCHN1\u003c\/strong\u003e, and \u003cstrong\u003eCMT1D\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":52952513741165,"sku":"E3928Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3928Hu.jpg?v=1769146493"},{"product_id":"human-e3-sumo-protein-ligase-nse2-nsmce2-elisa-kit-bhe12105403","title":"Human E3 Sumo-protein Ligase Nse2, NSMCE2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Sumo-protein Ligase Nse2 (NSMCE2)\u003c\/strong\u003e is a molecular target commonly studied in epigenetics and nuclear signaling research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q96MF7\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Sumo-protein Ligase Nse2 (NSMCE2) 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 E3 Sumo-protein Ligase Nse2 (NSMCE2) 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\u003eE3 Sumo-protein Ligase Nse2 (NSMCE2) 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 E3 Sumo-protein Ligase Nse2 (NSMCE2) 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\u003eE3 Sumo-protein Ligase Nse2 (NSMCE2)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eC8orf36\u003c\/strong\u003e, \u003cstrong\u003eE3 SUMO-protein ligase NSE2\u003c\/strong\u003e, and \u003cstrong\u003eE3 SUMO-protein transferase NSE2\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":52952515707245,"sku":"E3970Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E3970Hu.jpg?v=1769146497"},{"product_id":"human-26s-proteasome-non-atpase-regulatory-subunit-4-psmd4-elisa-kit-bhe12106147","title":"Human 26S Proteasome Non-atpase Regulatory Subunit 4, PSMD4 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003e26S Proteasome Non-atpase Regulatory Subunit 4 (PSMD4)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P55036\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, 26S Proteasome Non-atpase Regulatory Subunit 4 (PSMD4) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of 26S Proteasome Non-atpase Regulatory Subunit 4 (PSMD4) 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\u003e26S Proteasome Non-atpase Regulatory Subunit 4 (PSMD4) 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 26S Proteasome Non-atpase Regulatory Subunit 4 (PSMD4) 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\u003e26S Proteasome Non-atpase Regulatory Subunit 4 (PSMD4)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e26S proteasome non-ATPase regulatory subunit 4\u003c\/strong\u003e, \u003cstrong\u003e26S proteasome regulatory subunit RPN10\u003c\/strong\u003e, and \u003cstrong\u003e26S proteasome regulatory subunit S5A\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":52952539890029,"sku":"E4874Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E4874Hu.jpg?v=1769146586"},{"product_id":"human-e3-ubiquitin-protein-ligase-amfr-amfr-elisa-kit-bhe12106573","title":"Human E3 Ubiquitin-protein Ligase Amfr, AMFR ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Amfr (AMFR)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q9UKV5\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Amfr (AMFR) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Amfr (AMFR) 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\u003eE3 Ubiquitin-protein Ligase Amfr (AMFR) 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 E3 Ubiquitin-protein Ligase Amfr (AMFR) 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\u003eE3 Ubiquitin-protein Ligase Amfr (AMFR)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAMF receptor\u003c\/strong\u003e, \u003cstrong\u003eAMFR\u003c\/strong\u003e, and \u003cstrong\u003eAutocrine motility factor receptor\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":52952558829933,"sku":"E5210Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5210Hu.jpg?v=1769146673"},{"product_id":"human-e3-ubiquitin-protein-ligase-chip-stub1-elisa-kit-bhe12106574","title":"Human E3 Ubiquitin-protein Ligase Chip, STUB1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Chip (STUB1)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q9UNE7\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Chip (STUB1) 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 E3 Ubiquitin-protein Ligase Chip (STUB1) 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\u003eE3 Ubiquitin-protein Ligase Chip (STUB1) 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 E3 Ubiquitin-protein Ligase Chip (STUB1) 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\u003eE3 Ubiquitin-protein Ligase Chip (STUB1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAntigen NY-CO-7\u003c\/strong\u003e, \u003cstrong\u003eCarboxy terminus of Hsp70-interacting protein\u003c\/strong\u003e, and \u003cstrong\u003eCHIP\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":52952558862701,"sku":"E5211Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5211Hu.jpg?v=1769146673"},{"product_id":"human-e3-ubiquitin-protein-ligase-hace1-hace1-elisa-kit-bhe12106575","title":"Human E3 Ubiquitin-protein Ligase Hace1, HACE1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Hace1 (HACE1)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q8IYU2\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Hace1 (HACE1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Hace1 (HACE1) 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\u003eE3 Ubiquitin-protein Ligase Hace1 (HACE1) 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 E3 Ubiquitin-protein Ligase Hace1 (HACE1) 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\u003eE3 Ubiquitin-protein Ligase Hace1 (HACE1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase HACE1\u003c\/strong\u003e, \u003cstrong\u003eHACE1\u003c\/strong\u003e, and \u003cstrong\u003eHECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 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":52952558895469,"sku":"E5212Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5212Hu.jpg?v=1769146674"},{"product_id":"human-e3-ubiquitin-protein-ligase-mdm2-mdm2-elisa-kit-bhe12106576","title":"Human E3 Ubiquitin-protein Ligase Mdm2, MDM2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Mdm2 (MDM2)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q00987\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Mdm2 (MDM2) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Mdm2 (MDM2) 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\u003eE3 Ubiquitin-protein Ligase Mdm2 (MDM2) 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 E3 Ubiquitin-protein Ligase Mdm2 (MDM2) 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\u003eE3 Ubiquitin-protein Ligase Mdm2 (MDM2)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eACTFS\u003c\/strong\u003e, \u003cstrong\u003eDouble minute 2 protein\u003c\/strong\u003e, and \u003cstrong\u003eE3 ubiquitin-protein ligase Mdm2\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":52952558961005,"sku":"E5213Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5213Hu.jpg?v=1769146674"},{"product_id":"human-e3-ubiquitin-protein-ligase-mib2-mib2-elisa-kit-bhe12106577","title":"Human E3 Ubiquitin-protein Ligase Mib2, MIB2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Mib2 (MIB2)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q96AX9\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Mib2 (MIB2) 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 E3 Ubiquitin-protein Ligase Mib2 (MIB2) 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\u003eE3 Ubiquitin-protein Ligase Mib2 (MIB2) 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 E3 Ubiquitin-protein Ligase Mib2 (MIB2) 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\u003eE3 Ubiquitin-protein Ligase Mib2 (MIB2)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase MIB2\u003c\/strong\u003e, \u003cstrong\u003eMIB2\u003c\/strong\u003e, and \u003cstrong\u003eMind bomb homolog 2\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":52952558993773,"sku":"E5214Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5214Hu.jpg?v=1769146675"},{"product_id":"human-e3-ubiquitin-protein-ligase-mylip-mylip-elisa-kit-bhe12106578","title":"Human E3 Ubiquitin-protein Ligase Mylip, MYLIP ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Mylip (MYLIP)\u003c\/strong\u003e is a molecular target commonly studied in signal transduction research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q8WY64\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Mylip (MYLIP) 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 E3 Ubiquitin-protein Ligase Mylip (MYLIP) 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\u003eE3 Ubiquitin-protein Ligase Mylip (MYLIP) 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 E3 Ubiquitin-protein Ligase Mylip (MYLIP) 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\u003eE3 Ubiquitin-protein Ligase Mylip (MYLIP)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase MYLIP\u003c\/strong\u003e, \u003cstrong\u003eIDOL\u003c\/strong\u003e, and \u003cstrong\u003eInducible degrader of the LDL-receptor\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":52952559026541,"sku":"E5215Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5215Hu.jpg?v=1769146675"},{"product_id":"human-e3-ubiquitin-protein-ligase-rad18-rad18-elisa-kit-bhe12106579","title":"Human E3 Ubiquitin-protein Ligase Rad18, RAD18 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Rad18 (RAD18)\u003c\/strong\u003e is a molecular target commonly studied in epigenetics and nuclear signaling research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q9NS91\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Rad18 (RAD18) 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 E3 Ubiquitin-protein Ligase Rad18 (RAD18) 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\u003eE3 Ubiquitin-protein Ligase Rad18 (RAD18) 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 E3 Ubiquitin-protein Ligase Rad18 (RAD18) 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\u003eE3 Ubiquitin-protein Ligase Rad18 (RAD18)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase RAD18\u003c\/strong\u003e, \u003cstrong\u003ehHR18\u003c\/strong\u003e, and \u003cstrong\u003ehRAD18\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":52952559059309,"sku":"E5216Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5216Hu.jpg?v=1769146676"},{"product_id":"human-e3-ubiquitin-protein-ligase-synoviolin-syvn1-elisa-kit-bhe12106580","title":"Human E3 Ubiquitin-protein Ligase Synoviolin, SYVN1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Synoviolin (SYVN1)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q86TM6\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Synoviolin (SYVN1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Synoviolin (SYVN1) 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\u003eE3 Ubiquitin-protein Ligase Synoviolin (SYVN1) 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 E3 Ubiquitin-protein Ligase Synoviolin (SYVN1) 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\u003eE3 Ubiquitin-protein Ligase Synoviolin (SYVN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eDER3\u003c\/strong\u003e, \u003cstrong\u003eE3 ubiquitin-protein ligase synoviolin\u003c\/strong\u003e, and \u003cstrong\u003eHRD1\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":52952559092077,"sku":"E5217Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5217Hu.jpg?v=1769146676"},{"product_id":"human-e3-ubiquitin-protein-ligase-trim63-trim63-elisa-kit-bhe12106581","title":"Human E3 Ubiquitin-protein Ligase Trim63, TRIM63 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Trim63 (TRIM63)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q969Q1\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Trim63 (TRIM63) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Trim63 (TRIM63) 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\u003eE3 Ubiquitin-protein Ligase Trim63 (TRIM63) 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 E3 Ubiquitin-protein Ligase Trim63 (TRIM63) 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\u003eE3 Ubiquitin-protein Ligase Trim63 (TRIM63)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase TRIM63\u003c\/strong\u003e, \u003cstrong\u003eIRF\u003c\/strong\u003e, and \u003cstrong\u003eIris RING finger 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":52952559124845,"sku":"E5218Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5218Hu.jpg?v=1769146678"},{"product_id":"human-e3-ubiquitin-protein-ligase-trim68-trim68-elisa-kit-bhe12106582","title":"Human E3 Ubiquitin-protein Ligase Trim68, TRIM68 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Trim68 (TRIM68)\u003c\/strong\u003e is a molecular target commonly studied in life science research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q6AZZ1\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Trim68 (TRIM68) 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 E3 Ubiquitin-protein Ligase Trim68 (TRIM68) 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\u003eE3 Ubiquitin-protein Ligase Trim68 (TRIM68) 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 E3 Ubiquitin-protein Ligase Trim68 (TRIM68) 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\u003eE3 Ubiquitin-protein Ligase Trim68 (TRIM68)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase TRIM68\u003c\/strong\u003e, \u003cstrong\u003eGC109\u003c\/strong\u003e, and \u003cstrong\u003eRING finger protein 137\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":52952559157613,"sku":"E5219Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5219Hu.jpg?v=1769146678"},{"product_id":"human-proteasome-activator-complex-subunit-1-psme1-elisa-kit-bhe12107310","title":"Human Proteasome Activator Complex Subunit 1, PSME1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eProteasome Activator Complex Subunit 1 (PSME1)\u003c\/strong\u003e is a molecular target commonly studied in cell biology and microbiology 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: Q06323\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Proteasome Activator Complex Subunit 1 (PSME1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Proteasome Activator Complex Subunit 1 (PSME1) 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\u003eProteasome Activator Complex Subunit 1 (PSME1) 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 Proteasome Activator Complex Subunit 1 (PSME1) 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\u003eProteasome Activator Complex Subunit 1 (PSME1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e11S regulator complex subunit alpha\u003c\/strong\u003e, \u003cstrong\u003eActivator of multicatalytic protease subunit 1\u003c\/strong\u003e, and \u003cstrong\u003eHEL-S-129m\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":52952595988845,"sku":"E5948Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5948Hu.jpg?v=1769146872"},{"product_id":"human-proteasome-activator-complex-subunit-3-psme3-elisa-kit-bhe12107311","title":"Human Proteasome Activator Complex Subunit 3, PSME3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eProteasome Activator Complex Subunit 3 (PSME3)\u003c\/strong\u003e is a molecular target commonly studied in cell biology, immunology, and cancer 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: P61289\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Proteasome Activator Complex Subunit 3 (PSME3) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Proteasome Activator Complex Subunit 3 (PSME3) 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\u003eProteasome Activator Complex Subunit 3 (PSME3) 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 Proteasome Activator Complex Subunit 3 (PSME3) 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\u003eProteasome Activator Complex Subunit 3 (PSME3)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e11S regulator complex subunit gamma\u003c\/strong\u003e, \u003cstrong\u003eActivator of multicatalytic protease subunit 3\u003c\/strong\u003e, and \u003cstrong\u003eHEL-S-283\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":52952596021613,"sku":"E5949Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E5949Hu.jpg?v=1769146872"},{"product_id":"human-ring-finger-protein-207-rnf207-elisa-kit-bhe12107463","title":"Human Ring Finger Protein 207, RNF207 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eRing Finger Protein 207 (RNF207)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q6ZRF8\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ring Finger Protein 207 (RNF207) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Ring Finger Protein 207 (RNF207) 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\u003eRing Finger Protein 207 (RNF207) 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 Ring Finger Protein 207 (RNF207) 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\u003eRing Finger Protein 207 (RNF207)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eRING finger protein 207\u003c\/strong\u003e, \u003cstrong\u003eRNF 207\u003c\/strong\u003e, and \u003cstrong\u003eRNF207\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":52952599822701,"sku":"E6101Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6101Hu.jpg?v=1769146902"},{"product_id":"human-small-ubiquitin-related-modifier-1-sumo1-elisa-kit-bhe12107545","title":"Human Small Ubiquitin-related Modifier 1, SUMO1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSmall Ubiquitin-related Modifier 1 (SUMO1)\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: P63165\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Small Ubiquitin-related Modifier 1 (SUMO1) 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 Small Ubiquitin-related Modifier 1 (SUMO1) 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\u003eSmall Ubiquitin-related Modifier 1 (SUMO1) 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 Small Ubiquitin-related Modifier 1 (SUMO1) 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\u003eSmall Ubiquitin-related Modifier 1 (SUMO1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eGAP-modifying protein 1\u003c\/strong\u003e, \u003cstrong\u003eGMP1\u003c\/strong\u003e, and \u003cstrong\u003eSentrin\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":52952602247533,"sku":"E6183Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6183Hu.jpg?v=1769146920"},{"product_id":"human-small-ubiquitin-related-modifier-2-sumo2-elisa-kit-bhe12107546","title":"Human Small Ubiquitin-related Modifier 2, SUMO2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eSmall Ubiquitin-related Modifier 2 (SUMO2)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P61956\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Small Ubiquitin-related Modifier 2 (SUMO2) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Small Ubiquitin-related Modifier 2 (SUMO2) 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\u003eSmall Ubiquitin-related Modifier 2 (SUMO2) 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 Small Ubiquitin-related Modifier 2 (SUMO2) 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\u003eSmall Ubiquitin-related Modifier 2 (SUMO2)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eHSMT3\u003c\/strong\u003e, \u003cstrong\u003eSentrin-2\u003c\/strong\u003e, and \u003cstrong\u003eSmall ubiquitin-related modifier 2\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":52952602280301,"sku":"E6184Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6184Hu.jpg?v=1769146922"},{"product_id":"human-ubiquitin-thioesterase-otub2-otub2-elisa-kit-bhe12107736","title":"Human Ubiquitin Thioesterase Otub2, OTUB2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin Thioesterase Otub2 (OTUB2)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q96DC9\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin Thioesterase Otub2 (OTUB2) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Ubiquitin Thioesterase Otub2 (OTUB2) 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\u003eUbiquitin Thioesterase Otub2 (OTUB2) 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 Ubiquitin Thioesterase Otub2 (OTUB2) 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\u003eUbiquitin Thioesterase Otub2 (OTUB2)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eC14orf137\u003c\/strong\u003e, \u003cstrong\u003eDeubiquitinating enzyme OTUB2\u003c\/strong\u003e, and \u003cstrong\u003eOTB2\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":52952607555949,"sku":"E6374Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6374Hu.jpg?v=1769146958"},{"product_id":"human-ubiquitin-associated-and-sh3-domain-containing-protein-a-ubash3a-elisa-kit-bhe12107737","title":"Human Ubiquitin-associated and Sh3 Domain-containing Protein A, UBASH3A ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-associated and Sh3 Domain-containing Protein A (UBASH3A)\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: P57075\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-associated and Sh3 Domain-containing Protein A (UBASH3A) 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 Ubiquitin-associated and Sh3 Domain-containing Protein A (UBASH3A) 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\u003eUbiquitin-associated and Sh3 Domain-containing Protein A (UBASH3A) 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 Ubiquitin-associated and Sh3 Domain-containing Protein A (UBASH3A) 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\u003eUbiquitin-associated and Sh3 Domain-containing Protein A (UBASH3A)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCbl-interacting protein 4\u003c\/strong\u003e, \u003cstrong\u003eCLIP4\u003c\/strong\u003e, and \u003cstrong\u003eSTS-2\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":52952607687021,"sku":"E6375Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6375Hu.jpg?v=1769146958"},{"product_id":"human-ubiquitin-conjugating-enzyme-e2-variant-1-ube2v1-elisa-kit-bhe12107738","title":"Human Ubiquitin-conjugating Enzyme E2 Variant 1, UBE2V1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-conjugating Enzyme E2 Variant 1 (UBE2V1)\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: Q13404\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-conjugating Enzyme E2 Variant 1 (UBE2V1) 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 Ubiquitin-conjugating Enzyme E2 Variant 1 (UBE2V1) 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\u003eUbiquitin-conjugating Enzyme E2 Variant 1 (UBE2V1) 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 Ubiquitin-conjugating Enzyme E2 Variant 1 (UBE2V1) 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\u003eUbiquitin-conjugating Enzyme E2 Variant 1 (UBE2V1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCROC-1\u003c\/strong\u003e, \u003cstrong\u003eTRAF6-regulated IKK activator 1 beta Uev1A\u003c\/strong\u003e, and \u003cstrong\u003eUBE 2V1\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":52952607719789,"sku":"E6376Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6376Hu.jpg?v=1769146959"},{"product_id":"human-ubiquitin-conjugating-enzyme-e2-variant-2-ube2v2-elisa-kit-bhe12107739","title":"Human Ubiquitin-conjugating Enzyme E2 Variant 2, UBE2V2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2)\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: Q15819\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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 Ubiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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\u003eUbiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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 Ubiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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\u003eUbiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eDDVit 1\u003c\/strong\u003e, \u003cstrong\u003eDDVIT1\u003c\/strong\u003e, and \u003cstrong\u003eDDVit-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":52952607883629,"sku":"E6377Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6377Hu.jpg?v=1769146959"},{"product_id":"human-ubiquitin-like-modifier-activating-enzyme-atg7-atg7-elisa-kit-bhe12107741","title":"Human Ubiquitin-like Modifier-activating Enzyme Atg7, ATG7 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-like Modifier-activating Enzyme Atg7 (ATG7)\u003c\/strong\u003e is a molecular target commonly studied in cell biology, neuroscience, and cancer 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: O95352\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-like Modifier-activating Enzyme Atg7 (ATG7) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Ubiquitin-like Modifier-activating Enzyme Atg7 (ATG7) 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\u003eUbiquitin-like Modifier-activating Enzyme Atg7 (ATG7) 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 Ubiquitin-like Modifier-activating Enzyme Atg7 (ATG7) 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\u003eUbiquitin-like Modifier-activating Enzyme Atg7 (ATG7)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAPG7L\u003c\/strong\u003e, \u003cstrong\u003eAPG7-LIKE\u003c\/strong\u003e, and \u003cstrong\u003eATG12-activating enzyme E1 ATG7\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":52952607916397,"sku":"E6379Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6379Hu.jpg?v=1769146959"},{"product_id":"human-ubiquitin-like-protein-atg12-atg12-elisa-kit-bhe12107742","title":"Human Ubiquitin-like Protein Atg12, ATG12 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-like Protein Atg12 (ATG12)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: O94817\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-like Protein Atg12 (ATG12) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Ubiquitin-like Protein Atg12 (ATG12) 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\u003eUbiquitin-like Protein Atg12 (ATG12) 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 Ubiquitin-like Protein Atg12 (ATG12) 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\u003eUbiquitin-like Protein Atg12 (ATG12)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAPG12\u003c\/strong\u003e, \u003cstrong\u003eAPG12L\u003c\/strong\u003e, and \u003cstrong\u003eAPG12-like\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":52952607949165,"sku":"E6380Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6380Hu.jpg?v=1769146959"},{"product_id":"human-probable-e3-ubiquitin-protein-ligase-makorin-3-mkrn3-elisa-kit-bhe12107797","title":"Human Probable E3 Ubiquitin-protein Ligase Makorin-3, MKRN3 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eProbable E3 Ubiquitin-protein Ligase Makorin-3 (MKRN3)\u003c\/strong\u003e is a molecular target commonly studied in life science research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q13064\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Probable E3 Ubiquitin-protein Ligase Makorin-3 (MKRN3) 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 Probable E3 Ubiquitin-protein Ligase Makorin-3 (MKRN3) 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\u003eProbable E3 Ubiquitin-protein Ligase Makorin-3 (MKRN3) 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 Probable E3 Ubiquitin-protein Ligase Makorin-3 (MKRN3) 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\u003eProbable E3 Ubiquitin-protein Ligase Makorin-3 (MKRN3)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eCPPB2\u003c\/strong\u003e, \u003cstrong\u003eD15S9\u003c\/strong\u003e, and \u003cstrong\u003eMKRN3\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":52952609423725,"sku":"E6435Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6435Hu.jpg?v=1769146968"},{"product_id":"mouse-beclin-1-becn1-elisa-kit-bhe12109000","title":"Mouse Beclin 1, BECN1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBeclin 1 (BECN1)\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: O88597\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Beclin 1 (BECN1) 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 Beclin 1 (BECN1) 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\u003eBeclin 1 (BECN1) 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 Beclin 1 (BECN1) 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\u003eBeclin 1 (BECN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eBeclin-1\u003c\/strong\u003e, \u003cstrong\u003eBeclin-1-C 35 kDa\u003c\/strong\u003e, and \u003cstrong\u003eBeclin-1-C 37 kDa\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":52952618205549,"sku":"E1134Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1134Mo.jpg?v=1769147043"},{"product_id":"mouse-autophagy-protein-5-atg5-elisa-kit-bhe12109677","title":"Mouse Autophagy Protein 5, ATG5 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAutophagy Protein 5 (ATG5)\u003c\/strong\u003e is a molecular target commonly studied in cell biology, neuroscience, and cancer 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: Q99J83\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Autophagy Protein 5 (ATG5) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Autophagy Protein 5 (ATG5) 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\u003eAutophagy Protein 5 (ATG5) 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 Autophagy Protein 5 (ATG5) 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\u003eAutophagy Protein 5 (ATG5)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eAPG5-like\u003c\/strong\u003e, \u003cstrong\u003eATG 5\u003c\/strong\u003e, and \u003cstrong\u003eATG5\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":52952632361325,"sku":"E1865Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1865Mo.jpg?v=1769147121"},{"product_id":"mouse-e3-ubiquitin-protein-ligase-huwe1-huwe1-elisa-kit-bhe12109845","title":"Mouse E3 Ubiquitin-protein Ligase Huwe1, HUWE1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Huwe1 (HUWE1)\u003c\/strong\u003e is a molecular target commonly studied in life science research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q7TMY8\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Huwe1 (HUWE1) 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 E3 Ubiquitin-protein Ligase Huwe1 (HUWE1) 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\u003eE3 Ubiquitin-protein Ligase Huwe1 (HUWE1) 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 E3 Ubiquitin-protein Ligase Huwe1 (HUWE1) 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\u003eE3 Ubiquitin-protein Ligase Huwe1 (HUWE1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase HUWE1\u003c\/strong\u003e, \u003cstrong\u003eE3Histone\u003c\/strong\u003e, and \u003cstrong\u003eHECT, UBA and WWE domain-containing protein 1\u003c\/strong\u003e in publications and databases. Nomenclature differences and species context can influence how results are compared across studies.\u003c\/p\u003e","brand":"Bioassay Technology Laboratory","offers":[{"title":"96T","offer_id":52952637473133,"sku":"E2034Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2034Mo.jpg?v=1769147154"},{"product_id":"mouse-e3-ubiquitin-protein-ligase-parkin-park2-elisa-kit-bhe12109846","title":"Mouse E3 Ubiquitin-protein Ligase Parkin, PARK2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Parkin (PRKN)\u003c\/strong\u003e is a molecular target commonly studied in neuroscience and cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q9WVS6\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Parkin (PRKN) 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 E3 Ubiquitin-protein Ligase Parkin (PRKN) 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\u003eE3 Ubiquitin-protein Ligase Parkin (PRKN) 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 E3 Ubiquitin-protein Ligase Parkin (PRKN) 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\u003eE3 Ubiquitin-protein Ligase Parkin (PRKN)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase parkin\u003c\/strong\u003e, \u003cstrong\u003eParkin RBR E3 ubiquitin-protein ligase\u003c\/strong\u003e, and \u003cstrong\u003ePRKN\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":52952637505901,"sku":"E2035Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2035Mo.jpg?v=1769147154"},{"product_id":"mouse-e3-ubiquitin-protein-ligase-smurf1-smurf1-elisa-kit-bhe12109847","title":"Mouse E3 Ubiquitin-protein Ligase Smurf1, SMURF1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Smurf1 (SMURF1)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q9CUN6\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Smurf1 (SMURF1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Smurf1 (SMURF1) 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\u003eE3 Ubiquitin-protein Ligase Smurf1 (SMURF1) 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 E3 Ubiquitin-protein Ligase Smurf1 (SMURF1) 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\u003eE3 Ubiquitin-protein Ligase Smurf1 (SMURF1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase SMURF1\u003c\/strong\u003e, \u003cstrong\u003eHECT-type E3 ubiquitin transferase SMURF1\u003c\/strong\u003e, and \u003cstrong\u003eSMAD ubiquitination regulatory factor 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":52952637571437,"sku":"E2036Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2036Mo.jpg?v=1769147154"},{"product_id":"mouse-ubiquitin-like-modifier-activating-enzyme-1-uba1-elisa-kit-bhe12110362","title":"Mouse Ubiquitin-like Modifier-activating Enzyme 1, UBA1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-like Modifier-activating Enzyme 1 (UBA1)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q02053\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-like Modifier-activating Enzyme 1 (UBA1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Ubiquitin-like Modifier-activating Enzyme 1 (UBA1) 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\u003eUbiquitin-like Modifier-activating Enzyme 1 (UBA1) 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 Ubiquitin-like Modifier-activating Enzyme 1 (UBA1) 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\u003eUbiquitin-like Modifier-activating Enzyme 1 (UBA1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eA1\u003c\/strong\u003e, \u003cstrong\u003eA1S9\u003c\/strong\u003e, and \u003cstrong\u003eSb\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":52952657854829,"sku":"E2551Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2551Mo.jpg?v=1769147280"},{"product_id":"mouse-ubiquitin-like-protein-isg15-isg15-elisa-kit-bhe12110363","title":"Mouse Ubiquitin-like Protein Isg15, ISG15 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-like Protein Isg15 (ISG15)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. This molecule is commonly investigated as part of broader signaling, regulatory, or homeostatic networks.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q64339\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-like Protein Isg15 (ISG15) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Ubiquitin-like Protein Isg15 (ISG15) 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\u003eUbiquitin-like Protein Isg15 (ISG15) 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 Ubiquitin-like Protein Isg15 (ISG15) 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\u003eUbiquitin-like Protein Isg15 (ISG15)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eG1P2\u003c\/strong\u003e, \u003cstrong\u003ehUCRP\u003c\/strong\u003e, and \u003cstrong\u003ehUCRPIP17\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":52952657887597,"sku":"E2552Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2552Mo.jpg?v=1769147280"},{"product_id":"porcine-ubiquitin-carboxyl-terminalhydrolase-isozyme-l1-uchl1-elisa-kit-bhe12110984","title":"Porcine Ubiquitin Carboxyl-terminalhydrolase Isozyme L1, UCHL1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin Carboxyl-terminalhydrolase Isozyme L1 (UCHL1)\u003c\/strong\u003e is a molecular target commonly studied in neuroscience, cell biology, and tags \u0026amp; cell markers 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: Q6SEG5\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin Carboxyl-terminalhydrolase Isozyme L1 (UCHL1) 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 Ubiquitin Carboxyl-terminalhydrolase Isozyme L1 (UCHL1) 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\u003eUbiquitin Carboxyl-terminalhydrolase Isozyme L1 (UCHL1) 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 Ubiquitin Carboxyl-terminalhydrolase Isozyme L1 (UCHL1) 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\u003eUbiquitin Carboxyl-terminalhydrolase Isozyme L1 (UCHL1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eUbiquitin carboxyl-terminal hydrolase isozyme L1\u003c\/strong\u003e, \u003cstrong\u003eUbiquitin thioesterase L1\u003c\/strong\u003e, and \u003cstrong\u003eUCHL1\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":52952664179053,"sku":"E0611Po-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0611Po.jpg?v=1769147327"},{"product_id":"rat-beclin-1-becn1-elisa-kit-bhe12112148","title":"Rat Beclin 1, BECN1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eBeclin 1 (BECN1)\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: Q91XJ1\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Beclin 1 (BECN1) 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 Beclin 1 (BECN1) 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\u003eBeclin 1 (BECN1) 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 Beclin 1 (BECN1) 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\u003eBeclin 1 (BECN1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eBeclin-1\u003c\/strong\u003e, \u003cstrong\u003eBeclin-1-C 35 kDa\u003c\/strong\u003e, and \u003cstrong\u003eBeclin-1-C 37 kDa\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":52952678891885,"sku":"E0897Ra-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E0897Ra.jpg?v=1769147403"},{"product_id":"rat-autophagy-protein-5-atg5-elisa-kit-bhe12112775","title":"Rat Autophagy Protein 5, ATG5 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAutophagy Protein 5 (ATG5)\u003c\/strong\u003e is a molecular target commonly studied in cell biology, neuroscience, and cancer 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: Q3MQ06\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Autophagy Protein 5 (ATG5) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Autophagy Protein 5 (ATG5) 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\u003eAutophagy Protein 5 (ATG5) 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 Autophagy Protein 5 (ATG5) 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\u003eAutophagy Protein 5 (ATG5)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eATG5\u003c\/strong\u003e and \u003cstrong\u003eAutophagy protein 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":52952692949357,"sku":"E1547Ra-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1547Ra.jpg?v=1769147454"},{"product_id":"rat-e3-ubiquitin-protein-ligase-trim63-trim63-elisa-kit-bhe12113150","title":"Rat E3 Ubiquitin-protein Ligase Trim63, TRIM63 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Trim63 (TRIM63)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q91Z63\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Trim63 (TRIM63) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Trim63 (TRIM63) 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\u003eE3 Ubiquitin-protein Ligase Trim63 (TRIM63) 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 E3 Ubiquitin-protein Ligase Trim63 (TRIM63) 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\u003eE3 Ubiquitin-protein Ligase Trim63 (TRIM63)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase TRIM63\u003c\/strong\u003e, \u003cstrong\u003eMuRF1\u003c\/strong\u003e, and \u003cstrong\u003eMuRF-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":52952701665645,"sku":"E1951Ra-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E1951Ra.jpg?v=1769147509"},{"product_id":"rat-ubiquitin-carboxyl-terminal-hydrolase-isozyme-l1-uchl1-elisa-kit-bhe12113444","title":"Rat Ubiquitin Carboxyl-terminal Hydrolase Isozyme L1, UCHL1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin Carboxyl-terminal Hydrolase Isozyme L1 (UCHL1)\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: Q00981\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin Carboxyl-terminal Hydrolase Isozyme L1 (UCHL1) 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 Ubiquitin Carboxyl-terminal Hydrolase Isozyme L1 (UCHL1) 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\u003eUbiquitin Carboxyl-terminal Hydrolase Isozyme L1 (UCHL1) 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 Ubiquitin Carboxyl-terminal Hydrolase Isozyme L1 (UCHL1) 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\u003eUbiquitin Carboxyl-terminal Hydrolase Isozyme L1 (UCHL1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eNeuron cytoplasmic protein 9.5\u003c\/strong\u003e, \u003cstrong\u003ePGP 9.5\u003c\/strong\u003e, and \u003cstrong\u003ePGP9.5\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":52952711856493,"sku":"E2312Ra-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2312Ra.jpg?v=1769147563"},{"product_id":"rat-ubiquitin-conjugating-enzyme-e2-variant-2-ube2v2-elisa-kit-bhe12113445","title":"Rat Ubiquitin-conjugating Enzyme E2 Variant 2, UBE2V2 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eUbiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2)\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: Q7M767\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Ubiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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 Ubiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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\u003eUbiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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 Ubiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2) 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\u003eUbiquitin-conjugating Enzyme E2 Variant 2 (UBE2V2)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eMMS2\u003c\/strong\u003e, \u003cstrong\u003eUBE2V2\u003c\/strong\u003e, and \u003cstrong\u003eUbiquitin-conjugating enzyme E2 variant 2\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":52952711889261,"sku":"E2313Ra-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2313Ra.jpg?v=1769147563"},{"product_id":"human-e3-ubiquitin-protein-ligase-dtx3l-dtx3l-elisa-kit-bhe12115258","title":"Human E3 Ubiquitin-protein Ligase Dtx3L, DTX3L ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Dtx3L (DTX3L)\u003c\/strong\u003e is a molecular target commonly studied in epigenetics and nuclear signaling research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q8TDB6\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Dtx3L (DTX3L) 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 E3 Ubiquitin-protein Ligase Dtx3L (DTX3L) 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\u003eE3 Ubiquitin-protein Ligase Dtx3L (DTX3L) 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 E3 Ubiquitin-protein Ligase Dtx3L (DTX3L) 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\u003eE3 Ubiquitin-protein Ligase Dtx3L (DTX3L)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eBBAP\u003c\/strong\u003e, \u003cstrong\u003eB-lymphoma- and BAL-associated protein\u003c\/strong\u003e, and \u003cstrong\u003eDTX3L\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":52952719917421,"sku":"E7314Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E7314Hu.jpg?v=1769147600"},{"product_id":"human-e3-ubiquitin-protein-ligase-trim21-trim21-elisa-kit-bhe12115277","title":"Human E3 Ubiquitin-protein Ligase Trim21, TRIM21 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Trim21 (TRIM21)\u003c\/strong\u003e is a molecular target commonly studied in epigenetics and nuclear signaling and immunology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: P19474\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Trim21 (TRIM21) 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 E3 Ubiquitin-protein Ligase Trim21 (TRIM21) 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\u003eE3 Ubiquitin-protein Ligase Trim21 (TRIM21) 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 E3 Ubiquitin-protein Ligase Trim21 (TRIM21) 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\u003eE3 Ubiquitin-protein Ligase Trim21 (TRIM21)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e52 kDa ribonucleoprotein autoantigen Ro\/SS-A\u003c\/strong\u003e, \u003cstrong\u003e52 kDa Ro protein\u003c\/strong\u003e, and \u003cstrong\u003eE3 ubiquitin-protein ligase TRIM21\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":52952720736621,"sku":"E6796Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6796Hu.jpg?v=1769147605"},{"product_id":"human-e3-ubiquitin-protein-ligase-smurf1-smurf1-elisa-kit-bhe12115322","title":"Human E3 Ubiquitin-protein Ligase Smurf1, SMURF1 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eE3 Ubiquitin-protein Ligase Smurf1 (SMURF1)\u003c\/strong\u003e is a molecular target commonly studied in cell biology research. Immunoglobulins are antibody proteins central to humoral immunity and antigen recognition.\u003c\/p\u003e\u003cp\u003e\u003cstrong\u003eUniProt\u003c\/strong\u003e: Q9HCE7\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, E3 Ubiquitin-protein Ligase Smurf1 (SMURF1) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of E3 Ubiquitin-protein Ligase Smurf1 (SMURF1) 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\u003eE3 Ubiquitin-protein Ligase Smurf1 (SMURF1) 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 E3 Ubiquitin-protein Ligase Smurf1 (SMURF1) 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\u003eE3 Ubiquitin-protein Ligase Smurf1 (SMURF1)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003eE3 ubiquitin-protein ligase SMURF1\u003c\/strong\u003e, \u003cstrong\u003eHECT-type E3 ubiquitin transferase SMURF1\u003c\/strong\u003e, and \u003cstrong\u003ehSMURF1\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":52952722997613,"sku":"E6630Hu-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E6630Hu.jpg?v=1769147616"},{"product_id":"mouse-autophagy-related-protein-10-atg10-elisa-kit-bhe12115398","title":"Mouse Autophagy Related Protein 10, ATG10 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAutophagy Related Protein 10 (ATG10)\u003c\/strong\u003e is a molecular target commonly studied in cell biology, neuroscience, and cancer 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: Q8R1P4\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Autophagy Related Protein 10 (ATG10) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Autophagy Related Protein 10 (ATG10) 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\u003eAutophagy Related Protein 10 (ATG10) 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 Autophagy Related Protein 10 (ATG10) 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\u003eAutophagy Related Protein 10 (ATG10)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e5330424L23Rik\u003c\/strong\u003e, \u003cstrong\u003e5430428K15Rik\u003c\/strong\u003e, and \u003cstrong\u003eAgp10\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":52952727781741,"sku":"E2643Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2643Mo.jpg?v=1769147640"},{"product_id":"mouse-autophagy-related-protein-12-atg12-elisa-kit-bhe12115399","title":"Mouse Autophagy Related Protein 12, ATG12 ELISA Kit","description":"\u003ch2\u003eBackground\u003c\/h2\u003e\u003cp\u003e\u003cstrong\u003eAutophagy Related Protein 12 (ATG12)\u003c\/strong\u003e is a molecular target commonly studied in cell biology, cancer, and 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: Q9CQY1\u003c\/p\u003e\u003ch2\u003eBiological role and pathway context\u003c\/h2\u003e\u003cp\u003eIn the literature, Autophagy Related Protein 12 (ATG12) is frequently examined in relation to signal transduction pathways, cell cycle and stress-response programs, and organelle and membrane dynamics. Depending on the model system, changes in abundance can be associated with shifts in signaling state, cellular composition, or tissue physiology.\u003c\/p\u003e\u003ch2\u003eExpression and regulation\u003c\/h2\u003e\u003cp\u003eExpression of Autophagy Related Protein 12 (ATG12) 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\u003eAutophagy Related Protein 12 (ATG12) 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 Autophagy Related Protein 12 (ATG12) 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\u003eAutophagy Related Protein 12 (ATG12)\u003c\/strong\u003e may also be referred to as \u003cstrong\u003e4931423H11Rik\u003c\/strong\u003e, \u003cstrong\u003eA330058M13Rik\u003c\/strong\u003e, and \u003cstrong\u003eApg\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":52952727814509,"sku":"E2644Mo-96T","price":458.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/E2644Mo.jpg?v=1769147640"}],"url":"https:\/\/www.ebiohippo.com\/collections\/rs-ubiquitin-proteasome-system.oembed?page=15","provider":"BioHippo","version":"1.0","type":"link"}