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A3672

Sigma-Aldrich

Azurin

from Pseudomonas aeruginosa, lyophilized powder

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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)
Nadav Amdursky et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(2), 507-512 (2012-12-26)
Measuring solid-state electron transport (ETp) across proteins allows studying electron transfer (ET) mechanism(s), while minimizing solvation effects on the process. ETp is, however, sensitive to any static (conformational) or dynamic (vibrational) changes in the protein. Our macroscopic measurements allow extending
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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