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Merck
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A3641

Sigma-Aldrich

去铁铁蛋白 来源于马脾脏

0.2 μm filtered

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About This Item

CAS號碼:
MDL號碼:
分類程式碼代碼:
12352202
NACRES:
NA.32

品質等級

無菌

0.2 μm filtered

形狀

liquid

分子量

major subunit ML 19,889
minor subunit MH 22,200
native ~481.2 kDa (24 subunits, approx. 20 kDa each)

顏色

clear to slightly hazy, solution

儲存溫度

2-8°C

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應用

脱铁铁蛋白(来自马脾脏)已用于:
  • 测定其在相系统中的分配系数
  • 溶于NaCl用于培养细胞的铁装载
  • 在原位液体扫描透射电镜中用于生物学和纳米技术的界面成像

生化/生理作用

这种缺铁铁蛋白的蛋白质外鞘广泛用于凝胶过滤柱和十二烷基硫酸钠(SDS)-聚丙烯酰胺凝胶电泳的校准。 它在胰腺的β细胞中非常丰富,在那里充当抗氧化剂。添加到培养的内皮细胞中后,去铁铁蛋白以剂量反应方式摄取,保护细胞免受氧化剂介导的细胞溶解。

外觀

0.135 M氯化钠溶液。

儲存類別代碼

10 - Combustible liquids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves


分析證明 (COA)

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Hamish G Brown et al.
Communications biology, 5(1), 817-817 (2022-08-15)
Ice thickness is arguably one of the most important factors limiting the resolution of protein structures determined by cryo-electron microscopy (cryo-EM). The amorphous atomic structure of the ice that stabilizes and protects biological samples in cryo-EM grids also imprints some
Jan-Philip Wieferig et al.
IUCrJ, 8(Pt 2), 186-194 (2021-03-13)
As cryo-EM approaches the physical resolution limits imposed by electron optics and radiation damage, it becomes increasingly urgent to address the issues that impede high-resolution structure determination of biological specimens. One of the persistent problems has been beam-induced movement, which
M J MacDonald et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 8(10), 777-781 (1994-07-01)
In screening a rat pancreatic islet cDNA library by differential hybridization for transcripts increased by glucose, the H chain of ferritin, an iron storage protein, was identified. An ELISA for rat ferritin showed that the insulin cell contains a surprisingly
Ferritin-iron increases killing of Chinese hamster ovary cells by X-irradiation
Nelson JM and Stevens RG
Cell proliferation, 25(6), 579-585 (1992)
Cecilia Pozzi et al.
Proceedings of the National Academy of Sciences of the United States of America, 114(10), 2580-2585 (2017-02-17)
X-ray structures of homopolymeric L-ferritin obtained by freezing protein crystals at increasing exposure times to a ferrous solution showed the progressive formation of a triiron cluster on the inner cage surface of each subunit. After 60 min exposure, a fully

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