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Merck

A3641

Apoferritin from equine spleen

0.2 μm filtered

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About This Item

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

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Product Name

Apoferritin from equine spleen, 0.2 μm filtered

sterility

0.2 μm filtered

form

liquid

mol wt

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

color

clear to slightly hazy, solution

storage temp.

2-8°C

Quality Level

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This Item
F4503A9460V8379
mol wt

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

mol wt

H subunit ~21 kDa, L subunit ~19 kDa

mol wt

33 kDa (four subunits)

mol wt

A subunit 75 kDa, B subunit 65 kDa

form

liquid

form

saline solution

form

buffered aqueous solution

form

lyophilized powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−70°C

storage temp.

2-8°C

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

300

sterility

0.2 μm filtered

sterility

sterile-filtered

sterility

-

sterility

-

color

clear to slightly hazy, solution

color

red to brown

color

-

color

-

Application

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]

Biochem/physiol Actions

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]

Physical form

Solution in 0.135 M sodium chloride.

Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves


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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
Masahide Takehara et al.
Analytical biochemistry, 373(2), 322-329 (2007-12-07)
Two kinds of layer silicate powder, Micromica and chlorite, were used to aid protein crystallization by the addition to hanging drops. Using appropriate crystallization buffers, Micromica powder facilitated crystal growth speed for most proteins tested in this study. Furthermore, the
G Balla et al.
The Journal of biological chemistry, 267(25), 18148-18153 (1992-09-05)
Phagocyte-mediated oxidant damage to vascular endothelium is likely involved in various vasculopathies including atherosclerosis and pulmonary leak syndromes such as adult respiratory distress syndrome. We have shown that heme, a hydrophobic iron chelate, is rapidly incorporated into endothelial cells where
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

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