Ugrás a tartalomra
Merck

H17082

Sigma-Aldrich

2-Hydrazinopyridine

97%

Szinonimák:

2-Pyridylhydrazine

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Tapasztalati képlet (Hill-képlet):
C5H7N3
CAS-szám:
Molekulatömeg:
109.13
Beilstein:
109984
EC-szám:
MDL-szám:
UNSPSC kód:
12352100
PubChem Substance ID:
NACRES:
NA.22

Minőségi szint

Teszt

97%

bp

90-92 °C/1 mmHg (lit.)

mp

41-44 °C (lit.)

tárolási hőmérséklet

2-8°C

SMILES string

NNc1ccccn1

InChI

1S/C5H7N3/c6-8-5-3-1-2-4-7-5/h1-4H,6H2,(H,7,8)

Nemzetközi kémiai azonosító kulcs

NWELCUKYUCBVKK-UHFFFAOYSA-N

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Alkalmazás

  • Enhanced Metal Removal: Utilizing Schiff base functionalized dialdehyde starch, derived from 2-hydrazinopyridine, demonstrated significant potential in enhancing the removal of Cu(II) from solutions. The study included preparation methodologies, performance evaluations, and DFT calculations, showcasing its efficacy in water treatment technologies (Liang et al., 2024).
  • Dual Sensing Probe Development: A novel dicyanisophorone-based probe, incorporating 2-hydrazinopyridine, was developed for the dual sensing of Zn(2+) and Cd(2+) via near-infrared fluorescence. This advancement aids in the detection and analysis of heavy metals in various environmental and biological samples (Yan et al., 2023).
  • Active Site Analysis in Lysyl Oxidase: The study provided insights into the spatial arrangement of active site components in Lysyl Oxidase-like 2, including the role of 2-hydrazinopyridine, which is critical for understanding the enzyme′s mechanism and potential therapeutic applications (Meier et al., 2022).
  • Structural Analysis of Lysyl Oxidase: Research focused on the predicted 3D structure of the amine oxidase domain of Lysyl Oxidase-Like 2, exploring the interaction dynamics facilitated by 2-hydrazinopyridine. This contributes significantly to the field of molecular biology and enzyme function analysis (Meier et al., 2022).

Piktogramok

Exclamation mark

Figyelmeztetés

Warning

Figyelmeztető mondatok

Veszélyességi osztályok

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Célzott szervek

Respiratory system

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

230.0 °F - closed cup

Lobbanási pont (C)

110 °C - closed cup

Egyéni védőeszköz

dust mask type N95 (US), Eyeshields, Gloves


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Analitikai tanúsítványok (COA)

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Dokumentumtár megtekintése

D Collison et al.
The Biochemical journal, 264(3), 663-669 (1989-12-15)
Amine oxidase from pig plasma (PPAO) has two bound Cu2+ ions and at least one pyrroloquinoline quinone (PQQ) moiety as cofactors. It is shown that recovery of activity by copper-depleted PPAO is linear with respect to added Cu2+ ions. Recovery
Christian R P Kurtis et al.
Journal of neural transmission (Vienna, Austria : 1996), 118(7), 1043-1053 (2011-05-07)
Copper amine oxidases are important for the metabolism of a range of biogenic amines. Here, we focus on substrate specificity in the E. coli copper amine oxidase (ECAO) and specifically the role of Tyr 381. This residue, and its equivalent
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
Sudath Hapuarachchige et al.
Journal of the American Chemical Society, 133(17), 6780-6790 (2011-04-09)
A new class of fluorescent triazaborolopyridinium compounds was synthesized from hydrazones of 2-hydrazinylpyridine (HPY) and evaluated as potential dyes for live-cell imaging applications. The HPY dyes are small, their absorption/emission properties are tunable through variation of pyridyl or hydrazone substituents
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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