추천 제품
생물학적 소스
Pseudomonas aeruginosa
Quality Level
양식
lyophilized powder
구성
Protein, ≥65% Lowry
농도
≥65.0% (Lowry)
기술
toxicology assay: suitable
solubility
water: soluble 1—1.1 mg/mL, clear, blue (light blue to blue)
UniProt 수납 번호
저장 온도
−20°C
유전자 정보
Pseudomonas aeruginosa ... AZU(878046)
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일반 설명
Research area: Apoptosis. Azurinis a periplasmic protein and is a homotetramer.
애플리케이션
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
생화학적/생리학적 작용
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.
물리적 형태
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
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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시험 성적서(COA)
Lot/Batch Number
Bacterial redox protein azurin induce apoptosis in human osteosarcoma U2OS cells
Yang DS, et al.
Pharmacological Research, 52(5), 413-421 (2005)
Daniel Raimunda et al.
Metallomics : integrated biometal science, 5(2), 144-151 (2013-01-29)
Pseudomonas aeruginosa, an opportunistic pathogen, has two transmembrane Cu(+) transport ATPases, CopA1 and CopA2. Both proteins export cytoplasmic Cu(+) into the periplasm and mutation of either gene leads to attenuation of virulence. CopA1 is required for maintaining cytoplasmic copper levels
Matthew P McLaughlin et al.
Journal of the American Chemical Society, 134(48), 19746-19757 (2012-11-22)
The apoprotein of Pseudomonas aeruginosa azurin binds iron(II) to give a 1:1 complex, which has been characterized by electronic absorption, Mössbauer, and NMR spectroscopies, as well as X-ray crystallography and quantum-chemical computations. Despite potential competition by water and other coordinating
Wenjie Li et al.
ACS nano, 6(12), 10816-10824 (2012-11-10)
Solid-state electron transport (ETp) via a monolayer of immobilized azurin (Az) was examined by conducting probe atomic force microscopy (CP-AFM), as a function of both temperature (248-373K) and applied tip force (6-15 nN). At low forces, ETp via holo-Az (with
Leandro Gammuto et al.
Microorganisms, 10(1) (2022-01-22)
Azurin is a bacterial-derived cupredoxin, which is mainly involved in electron transport reactions. Interest in azurin protein has risen in recent years due to its anticancer activity and its possible applications in anticancer therapies. Nevertheless, the attention of the scientific
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