联系我们
联系人：陈先生
产品展示
HMOX1 Human/ 重组人亚铁血红素加氧酶1
点击次数：385
价格：￥电议
更新日期：2026/8/24 23:18:11
生 产 地：欧洲
产品型号：
商家名片
陈**
联系我时，请说明是阿仪网看到的，谢谢!
- 电话: 05*******891
- 手机: 18******628
- 微信:
- 交换名片后展示联系方式 → →
相关标签：HMOX1,Human,重组人亚铁血红素加氧酶1
详细内容
慧嘉生物您实验身边的好伙伴
为客户提供“最高品质的产品”和“最优质的服务”
AssayBiotech CUSABIO Immunoway Santa Abcam Cst jackson Pierce Sigma Amresco Qiagen Cayman abnova millipore invitrogen merk ebioscience prospec lifespan BD
欢迎广大客户咨询，另有大量宣传海报和小礼品赠送。
网站：www..com
Q Q：
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
Synonyms HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. Introduction HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. Description HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. Source Escherichia Coli. Physical Appearance Sterile filtered colorless solution. Formulation HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. Stability HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C.
Please prevent freeze thaw cycles. Amino acid sequence MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. Purity Greater than 95.0% as determined by SDS-PAGE. Usage ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
HMOX1 Human/ 重组人亚铁血红素加氧酶1
产品编号：ENZ-392
产品规格：10μg/50μg/1mg
产品规格：10μg/50μg/1mg
| Synonyms | HO-1, HSP32, bK286B10, HMOX-1, Heme oxygenase 1, HMOX1, HO, HO1. |
| Introduction | HMOX1 cleaves the heme ring at the alpha methene bridge to form Biliverdin. Biliverdin is then converted to Bilirubin by Biliverdin reductase. In physiological state, the highest activity of HMOX1 is found in the spleen, where senescent erythrocytes are sequestrated ａnd destroyed. Heme Oxygenase-1 is involved in the regulation of cardiovascular function ａnd its adaptive response to a variety of stressors. HMOX1 is induced in the colon of ulcerative colitis. HMOX1 is found to overexpress with a higher extent of intraplaque angiogenesis implies a multi-faceted role for HMOX1 in modulating the progression of atherosclerosis. HMOX1 expression reduced LPS-stimulated secretion of MCP-1, IL-6, IL-10, ａnd TNF-alpha in murine ａnd human macrophages. |
| Description | HO-1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 274 amino acids （1-266） ａnd having a molecular mass of 31.4 kDa. HO-1 is fused to 8 amino acid His Tag at C-Terminus ａnd purified by proprietary chromatographic techniques. |
| Source | Escherichia Coli. |
| Physical Appearance | Sterile filtered colorless solution. |
| Formulation | HMOX1 solution containing 20mM Tris pH-8, 50mM NaCl, 0.1mM PMSF ａnd 10% glycerol. |
| Stability | HMOX1 Human Recombinant although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. |
| Amino acid sequence | MERPQPHSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALEQDLAFWYGPR WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQLYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV ETPRGKPPLN TRSQAPLEHHHHHH. |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Usage | ProSpec＇s products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals. |
HMOX1,Human,重组人亚铁血红素加氧酶1
