A3672
Azurin
from Pseudomonas aeruginosa, lyophilized powder
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About This Item
biological source
Pseudomonas aeruginosa
Quality Level
form
lyophilized powder
composition
Protein, ≥65% Lowry
concentration
≥65.0% (Lowry)
technique(s)
toxicology assay: suitable
solubility
water: soluble 1—1.1 mg/mL, clear, blue (light blue to blue)
UniProt accession no.
storage temp.
−20°C
Gene Information
Pseudomonas aeruginosa ... AZU(878046)
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General description
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
Biochem/physiol Actions
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.
Physical form
Lyophilized powder containing ammonium acetate buffer salts.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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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
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)
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
Caterina Bernini et al.
Journal of the American Chemical Society, 135(12), 4822-4833 (2013-03-06)
Many biological electron-transfer reactions involve short-lived tryptophan radicals as key reactive intermediates. While these species are difficult to investigate, the recent photogeneration of a long-lived neutral tryptophan radical in two Pseudomonas aeruginosa azurin mutants (Az48W and ReAz108W) made it possible
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