推荐产品
产品名称
Nα-乙酰基-L-鸟氨酸,
化驗
≥98% (TLC)
品質等級
形狀
powder
技術
ligand binding assay: suitable
顏色
colorless to white
儲存溫度
−20°C
SMILES 字串
CC(=O)N[C@@H](CCCN)C(O)=O
InChI
1S/C7H14N2O3/c1-5(10)9-6(7(11)12)3-2-4-8/h6H,2-4,8H2,1H3,(H,9,10)(H,11,12)/t6-/m0/s1
InChI 密鑰
JRLGPAXAGHMNOL-LURJTMIESA-N
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生化/生理作用
Nα-乙酰基-L-鸟氨酸 (AORN) 是鉴定、分化和表征植物、部分真细菌和一些人类病原体中存在的 N(α)-乙酰基-L-鸟氨酸脱乙酰基酶和N-乙酰基-L-鸟氨酸转氨酶(AOTCase)的底物。
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
Eyeshields, Gloves, type N95 (US)
其他客户在看
Amino acids, 51(8), 1103-1127 (2019-07-04)
Already very early, the study of microbial arginine biosynthesis and its regulation contributed significantly to the development of new ideas and concepts. Hence, the term "repression" was proposed by Vogel (The chemical basis of heredity, The John Hopkins Press, Baltimore
Plant & cell physiology, 56(11), 2158-2168 (2015-09-13)
The role of salicylic acid (SA) and jasmonic acid (JA) signaling in resistance to root pathogens has been poorly documented. We assessed the contribution of SA and JA to basal and partial resistance of Arabidopsis to the biotrophic clubroot agent
Proteins, 64(2), 532-542 (2006-06-03)
N-acetyl-L-ornithine transcarbamoylase (AOTCase) is a new member of the transcarbamoylase superfamily that is essential for arginine biosynthesis in several eubacteria. We report here crystal structures of the binary complexes of AOTCase with its substrates, carbamoyl phosphate (CP) or N-acetyl-L-ornithine (AORN)
The Journal of biological chemistry, 280(15), 14366-14369 (2005-02-26)
We have identified in Xanthomonas campestris a novel N-acetylornithine transcarbamylase that replaces ornithine transcarbamylase in the canonic arginine biosynthetic pathway of several Eubacteria. The crystal structures of the protein in the presence and absence of the reaction product, N-acetylcitrulline, were
Biochemistry, 49(32), 6887-6895 (2010-08-11)
N-Acetyl-l-ornithine transcarbamylase (AOTCase), rather than ornithine transcarbamylase (OTCase), is the essential carbamylase enzyme in the arginine biosynthesis of several plant and human pathogens. The specificity of this unique enzyme provides a potential target for controlling the spread of these pathogens.
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