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商品详情
名称
Recombinant Human Heme Oxygenase 1 Protein
别名
重组人血红素加氧酶 1 蛋白
英文别名
bK286B10 | EC 1.14.99.3 | heat shock protein, 32-kD | heme oxygenase (decycling) 1 | HMOX1 | HO | HO1 | HO-1 | HO-1heme oxygenase 1 | HSP32
货号
rp176715-1mg
包装规格
1mg
级别
无载体
浓度
≥98%(SDS-PAGE)
纯度
>98% (SDS-PAGE)
产品介绍
Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. The mechanism of HMOX is unique in that heme serves as the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HMOX activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HMOX1 and HMOX2, are expressed in most tissues. HMOX1 is an inducible enzyme in response to heme, heavy metals, oxidative stress, cytokines, and many drugs. Whereas HMOX2 displays a constitutive expression. HMOX1 is expressed mainly in spleen, liver, and kidney, and HMOX2 is prominently expressed in the brain and testes. The increased expression of HMOX1 levels is related to a variety of pathological states, where it functions as a cytoprotective molecule through its by products. HMOX1 also plays important roles in the regulation of cell proliferation, differentiation, and apoptosis.
来源
重组表达
预测分子量
30.7 kDa
蛋白标签
C-His
SDS-PAGE
28.8 kDa, reducing conditions; 28.8 kDa, non-reducing conditions
表达系统
E. coli Accession #: P09601 | E. coli
种属
人(Human)
氨基酸
1-261 aa
序列
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTHHHHHH
无动物源
No
无载体
Yes
危险属性
「暂无危险属性」
上下游信息
「暂无上下游信息」
技术文档
「暂无技术文档」
相关文章
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Recombinant Human Heme Oxygenase 1 Protein 无载体 1mg

品牌:阿拉丁
货号:rp176715-1mg
级别: 无载体
货期:30天
已售 483 件
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运费:0 元
规格:

1mg

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