A3672
天青蛋白
from Pseudomonas aeruginosa, lyophilized powder
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)
正在寻找类似产品? 访问 产品对比指南
General description
研究领域：细胞凋亡。天青蛋白是一种质周蛋白，是同型四聚体。
Application
天青素可用于：
- 骨肉瘤细胞系的细胞毒性和细胞活力研究
- 相互作用研究中氮化硅悬臂的功能化
- 氧化硅和云母的金表面和绝缘的功能化氧化物表面的涂层
Biochem/physiol Actions
在细菌反硝化过程中，天青蛋白作为亚硝酸盐还原酶的电子供体。天青蛋白表现出抗癌活性，因为它阻碍了与癌症进展相关的各种独立信号通路。它与肿瘤抑制蛋白p53结合，诱导癌细胞凋亡或阻止癌细胞生长。天青蛋白通过降低VEGFR-2酪氨酸激酶的活性来抑制肿瘤生长，从而破坏血管生成。已经观察到它在人类乳腺癌细胞和人类黑色素瘤细胞中显示出细胞毒性。
天青素是铜氧还蛋白家族中的金属蛋白。它比正常细胞优先进入癌细胞并诱导细胞凋亡。Azurin 与 ephrinB2 结构相似，并且实际上结合了 ephrin 受体酪氨酸激酶 EphB2 来启动参与癌症发展的细胞信号传导。天青素抑制 EphB2 酪氨酸残基的自磷酸化，干扰上游细胞信号传导并有助于抑制癌细胞生长。
Physical form
含有醋酸铵缓冲盐的冻干粉末。
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
此项目有
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
相关内容
Instructions
我们的科学家团队拥有各种研究领域经验，包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系客户支持