质量水平
方案
97%
沸点
90-92 °C/1 mmHg (lit.)
mp
41-44 °C (lit.)
储存温度
2-8°C
SMILES字符串
NNc1ccccn1
InChI
1S/C5H7N3/c6-8-5-3-1-2-4-7-5/h1-4H,6H2,(H,7,8)
InChI key
NWELCUKYUCBVKK-UHFFFAOYSA-N
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应用
- 增强金属去除功能：利用由2-肼吡啶衍生的希夫碱功能化双醛淀粉，在增强溶液中Cu(II)的去除方面显示出显著的潜力。该研究包括制备方法、性能评估和DFT计算，展示了其在水处理技术中的功效（Liang et al., 2024）。
- 双感测探头发展：研制了一种新型的含2-肼吡啶的双氰异佛隆探针，用于近红外荧光双传感Zn(2+)和Cd(2+)。这一进步有助于检测和分析各种环境和生物样品中的重金属（Yan et al., 2023）。
- 赖氨酸氧化酶活性位点分析：该研究深入了解了赖氨酸氧化酶样2活性位点组分的空间排列，包括2-肼吡啶的作用，这对于理解酶的机制和潜在的治疗应用至关重要（Meier et al., 2022）。
- 赖氨酸氧化酶的结构分析：研究重点是预测赖氨酸氧化酶样2的胺氧化酶结构域的三维结构，探索2-肼吡啶促进的相互作用动力学。这对分子生物学和酶功能分析领域意义重大（Meier et al., 2022）。
警示用语：
Warning
危险声明
危险分类
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
230.0 °F - closed cup
闪点(°C)
110 °C - closed cup
个人防护装备
dust mask type N95 (US), Eyeshields, Gloves
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
J M Murray et al.
Biochemistry, 40(43), 12808-12818 (2001-10-24)
Copper amine oxidases are homodimeric enzymes that catalyze two reactions: first, a self-processing reaction to generate the 2,4,5-trihydroxyphenylalanine (TPQ) cofactor from an active site tyrosine by a single turnover mechanism; second, the oxidative deamination of primary amine substrates with the
C M Wilmot et al.
Biochemistry, 36(7), 1608-1620 (1997-02-18)
The crystal structure of the complex between the copper amine oxidase from Escherichia coli (ECAO) and a covalently bound inhibitor, 2-hydrazinopyridine, has been determined to a resolution of 2.0 A. The inhibitor covalently binds at the 5 position of the
G De Matteis et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 4(3), 348-353 (1999-08-10)
Bovine serum amine oxidase (BSAO) reacts with 2-hydrazinopyridine, which binds the organic co-factor 2,4,5-trihydroxyphenylalanine quinone, forming a band at 435 nm. The band shifts to 526 nm around 60 degrees C, to 415 nm upon denaturation, but only shifts to
Minae Mure et al.
Biochemistry, 44(5), 1583-1594 (2005-02-03)
Adduct I (lambda(max) at approximately 430 nm) formed in the reaction of 2-hydrazinopyridine (2HP) and the TPQ cofactor of wild-type Escherichia coli copper amine oxidase (WT-ECAO) is stable at neutral pH, 25 degrees C, but slowly converts to another spectroscopically
Minae Mure et al.
Biochemistry, 44(5), 1568-1582 (2005-02-03)
2-Hydrazinopyridine (2HP) is an irreversible inhibitor of copper amine oxidases (CAOs). 2HP reacts directly at the C5 position of the TPQ cofactor, yielding an intense chromophore with lambda(max) approximately 430 nm (adduct I) in Escherichia coli amine oxidase (ECAO). The
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