H17082
2-Hydrazinopyridine
97%
Sinonimo/i:
2-Pyridylhydrazine
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
About This Item
Formula empirica (notazione di Hill):
C5H7N3
Numero CAS:
Peso molecolare:
109.13
Beilstein:
109984
Numero CE:
Numero MDL:
Codice UNSPSC:
12352100
ID PubChem:
NACRES:
NA.22
Prodotti consigliati
Saggio
97%
P. ebollizione
90-92 °C/1 mmHg (lit.)
Punto di fusione
41-44 °C (lit.)
Temperatura di conservazione
2-8°C
Stringa SMILE
NNc1ccccn1
InChI
1S/C5H7N3/c6-8-5-3-1-2-4-7-5/h1-4H,6H2,(H,7,8)
NWELCUKYUCBVKK-UHFFFAOYSA-N
Cerchi prodotti simili? Visita Guida al confronto tra prodotti
Categorie correlate
Applicazioni
- 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).
Avvertenze
Warning
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Organi bersaglio
Respiratory system
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
230.0 °F - closed cup
Punto d’infiammabilità (°C)
110 °C - closed cup
Dispositivi di protezione individuale
dust mask type N95 (US), Eyeshields, Gloves
Scegli una delle versioni più recenti:
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
E S H El Ashry et al.
Nucleosides, nucleotides & nucleic acids, 23(3), 567-580 (2004-04-29)
Reaction of 2-hydrazinopyridine (1) with D-xylose, D-galactose, D-glucose and D-fructose afforded the corresponding hydrazones mainly in the acyclic forms 2, 3, 6 and 11 with minor amounts of the cyclic structures. Oxidative cyclization of the hydrazones with bromine in methanol
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
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
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
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
Contatta l'Assistenza Tecnica.