A3672
Azurin
from Pseudomonas aeruginosa, lyophilized powder
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About This Item
Form:
lyophilized powder
Biological source:
Pseudomonas aeruginosa
biological source
Pseudomonas aeruginosa
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
Quality Level
Gene Information
Pseudomonas aeruginosa ... AZU(878046)
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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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
Comparison of the self-chemisorption of azurin on gold and on functionalized oxide surfaces
Schnyder BK, et al.
Surface and Interface Analysis : SIA, 34(1), 40-44 (2002)
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
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
Ryan G Hadt et al.
Journal of the American Chemical Society, 134(40), 16701-16716 (2012-09-19)
The reduction potentials (E(0)) of type 1 (T1) or blue copper (BC) sites in proteins and enzymes with identical first coordination spheres around the redox active copper ion can vary by ~400 mV. Here, we use a combination of low-temperature
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