The method of preparation is considered proprietary. However, as mentioned in this properties section of the Product Detail Page, this is Azurin from Pseudomonas aeruginosa. See the links below to review a sample Certificate of Analysis and the product data sheet, respectively:
https://www.sigmaaldrich.com/certificates/sapfs/PROD/sap/certificate_pdfs/COFA/Q14/A3672-1MG0000211689.pdf
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/306/100/a3672dat.pdf
A3672
Azurin
from Pseudomonas aeruginosa, lyophilized powder
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1 MG
CHF 765.00
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1 MG
CHF 765.00
About This Item
Prodotti consigliati
Origine biologica
Pseudomonas aeruginosa
Livello qualitativo
Stato
lyophilized powder
Composizione
Protein, ≥65% Lowry
Concentrazione
≥65.0% (Lowry)
tecniche
toxicology assay: suitable
Solubilità
water: soluble 1—1.1 mg/mL, clear, blue (light blue to blue)
N° accesso UniProt
Temperatura di conservazione
−20°C
Informazioni sul gene
Pseudomonas aeruginosa ... AZU(878046)
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Descrizione generale
Research area: Apoptosis. Azurinis a periplasmic protein and is a homotetramer.[1]
Applicazioni
Azioni biochim/fisiol
Azurin acts as an electron donor for nitrite reductase in bacterial denitrification process.[1] It exhibits anticancer activity[1] 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.[5]
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.
Stato fisico
Lyophilized powder containing ammonium acetate buffer salts.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
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Certificati d'analisi (COA)
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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)
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
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
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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How do i know that this is azurin i mean any confirmatory test or anything else.
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