A3672
Azurin
from Pseudomonas aeruginosa, lyophilized powder
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About This Item
Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61
Produits recommandés
Source biologique
Pseudomonas aeruginosa
Niveau de qualité
Forme
lyophilized powder
Composition
Protein, ≥65% Lowry
Concentration
≥65.0% (Lowry)
Technique(s)
toxicology assay: suitable
Solubilité
water: soluble 1—1.1 mg/mL, clear, blue (light blue to blue)
Numéro d'accès UniProt
Température de stockage
−20°C
Informations sur le gène
Pseudomonas aeruginosa ... AZU(878046)
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Description générale
Research area: Apoptosis. Azurinis a periplasmic protein and is a homotetramer.
Application
Azurin has been used:
- in the cytotoxicity and cell viability studies in human osteosarcoma cell line
- for the functionalization of silicon nitride cantilevers for interaction studies
- for coating gold surface and insulating functionalized oxide surfaces of silicon oxide and mica
Actions biochimiques/physiologiques
Azurin acts as an electron donor for nitrite reductase in bacterial denitrification process. It exhibits anticancer activity as it hampers various independent signaling pathways associated with cancer progression. It binds to tumor suppressor protein p53 and induces cancer cell apoptosis or stalls cancer cell growth. Azurin disrupts angiogenesis by reducing the activity of VEGFR-2tyrosine kinase thereby inhibiting tumor growth. It has been observed to show cytotoxicity in human breast cancer cells and human melanoma cells.
Azurin is a metalloprotein in the family of cupredoxins. It preferentially enters cancer cells over normal cells and induces apoptosis. Azurin has structural similarities to ephrinB2, and in fact binds the ephrin receptor tyrosine kinase EphB2 to initiate cell signaling that is involved in cancer progression. Azurin inhibits autophosphorlyation of the EphB2 tyrosine residue, interfering with upstream cell signaling and contributing to cancer cell growth inhibition.
Forme physique
Lyophilized powder containing ammonium acetate buffer salts.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Interaction of p53 with Mdm2 and azurin as studied by atomic force spectroscopy
Funari G, et al.
Journal of Molecular Recognition, 23(4), 343-351 (2010)
Marcel Swart et al.
Chemistry & biodiversity, 9(9), 1728-1738 (2012-09-15)
UV/VIS Electron excitation spectra have been computed for large, realistic model systems of the blue copper protein family. Fully quantum-chemical calculations at the density-functional theory level employing polarized triple-ζ basis sets have been performed on systems of over 120 atoms
Yunlei Zhang et al.
Applied and environmental microbiology, 78(21), 7603-7610 (2012-08-28)
Many studies have demonstrated that intravenously administered bacteria can target and proliferate in solid tumors and then quickly be released from other organs. Here, we employed the tumor-targeting property of Escherichia coli Nissle 1917 to inhibit mouse B16 melanoma and
Koyu Fujita et al.
Journal of inorganic biochemistry, 115, 163-173 (2012-08-23)
Pseudoazurin (PAz), a well-characterized blue copper electron-transfer protein, is shown herein to be capable of mediating electron transfer to the nitrous oxide reductase (N(2)OR) from Achromobacter cycloclastes (Ac). Spectroscopic measurements demonstrate that reduced PAz is efficiently re-oxidized by a catalytic
Ole Farver et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(26), 10536-10540 (2013-06-14)
Low reorganization free energies are necessary for fast electron transfer (ET) reactions. Hence, rational design of redox proteins with lower reorganization free energies has been a long-standing challenge, promising to yield a deeper understanding of the underlying principles of ET
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