推薦產品
生物源
spinach (Spinacia oleracea)
品質等級
形狀
buffered aqueous solution
濃度
1.0-3.0 mg/mL in 0.15 M Trizma buffer, pH 7.5 and NaCl (Frozen)
應用
cell analysis
運輸包裝
dry ice
儲存溫度
−70°C
基因資訊
spinach ... SOVF(137530)
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應用
铁氧还蛋白已用于研究在没有铵的情况下从亚硝酸盐或硝酸盐中同化无机氮。铁氧还蛋白在该氮同化所需的电子转移级联中具有重要作用。
生化／生理作用
铁氧还蛋白是一种含铁蛋白，可在光合作用和固氮作用中起电子转移催化剂的作用。
包裝
包装规格取决于铁氧还蛋白含量。
準備報告
通过 Tagawa 和 Arnon 在 Nature, 195, 537 (1962) 中介绍的方法部分纯化。
訊號詞
Warning
危險聲明
危險分類
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
標靶器官
Respiratory system
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
dust mask type N95 (US), Eyeshields, Gloves
分析證明 (COA)
輸入產品批次/批號來搜索 分析證明 (COA)。在產品’s標籤上找到批次和批號，寫有 ‘Lot’或‘Batch’.。
Rosa M Martínez-Espinosa et al.
Biochimica et biophysica acta, 1623(1), 47-51 (2003-09-06)
Haloferax mediterranei is a halophilic archaeon that can grow in aerobic conditions with nitrate as sole nitrogen source. The electron donor in the aerobic nitrate reduction to ammonium was a ferredoxin. This ferredoxin has been purified and characterised. Air-oxidized H.
Basilio Zafrilla et al.
Biochemical Society transactions, 39(6), 1844-1848 (2011-11-23)
In the absence of ammonium, many organisms, including the halophilic archaeon Haloferax volcanii DS2 (DM3757), may assimilate inorganic nitrogen from nitrate or nitrite, using a ferredoxin-dependent assimilatory NO₃⁻/NO₂⁻ reductase pathway. The small acidic ferredoxin Hv-Fd plays an essential role in
Rosa María Martínez-Espinosa et al.
FEMS microbiology letters, 277(1), 50-55 (2007-11-08)
Haloferax mediterranei is a halophilic archaeon that can grow using nitrate as the sole nitrogen source. A ferredoxin that serves as the physiological electron donor to the nitrate and nitrite reductases in this assimilatory process has been characterized. The ferredoxin
Pascal Belin et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(18), 7426-7431 (2009-05-07)
The gene encoding the cytochrome P450 CYP121 is essential for Mycobacterium tuberculosis. However, the CYP121 catalytic activity remains unknown. Here, we show that the cyclodipeptide cyclo(l-Tyr-l-Tyr) (cYY) binds to CYP121, and is efficiently converted into a single major product in
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