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Merck
모든 사진(1)

주요 문서

A3641

Sigma-Aldrich

Apoferritin from equine spleen

0.2 μm filtered

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About This Item

CAS Number:
MDL number:
UNSPSC 코드:
12352202
NACRES:
NA.32

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Quality Level

무균

0.2 μm filtered

양식

liquid

분자량

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

색상

clear to slightly hazy, solution

저장 온도

2-8°C

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애플리케이션

Apoferritin from equine spleen has been used:
  • to determine its partition coefficients in phase systems[1]
  • in NaCl for iron loading of cultured cells[2]
  • in in situ liquid scanning transmission electron microscope for imaging the interface of biology and nanotechnology[3]

생화학적/생리학적 작용

This protein shell of ferritin lacking iron is widely used for the calibration of gel filtration columns and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.[4] It is very abundant in beta-cells of the pancreas where it acts as an anti-oxidant.[5] When added to cultured endothelial cells apoferritin is taken up in a dose-responsive manner and appears to protect the cells from oxidant-mediated cytolysis. [6]

물리적 형태

Solution in 0.135 M sodium chloride.

Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves


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문서 라이브러리 방문

Visualizing macromolecular complexes with in situ liquid scanning transmission electron microscopy
Evans JE, et al.
Micron (Oxford, England : 1993), 43(11), 1085-1090 (2012)
Jorge H Melillo et al.
Scientific reports, 12(1), 16512-16512 (2022-10-04)
Some of the best nucleating agents in nature are ice-nucleating proteins, which boost ice growth better than any other material. They can induce immersion freezing of supercooled water only a few degrees below 0 °C. An open question is whether this
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
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
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

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