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S4920
SITE Liquid Media Supplement (100×)
liquid, sterile-filtered, BioReagent, suitable for cell culture
Synonym(e):
Media supplement
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5 ML
85,60 €
About This Item
UNSPSC-Code:
12352205
NACRES:
NA.75
Empfohlene Produkte
Sterilität
sterile-filtered
Produktlinie
BioReagent
Form
liquid
Methode(n)
cell culture | mammalian: suitable
Verunreinigungen
endotoxin, tested
Versandbedingung
ambient
Lagertemp.
2-8°C
Allgemeine Beschreibung
SITE Liquid Media Supplement (100×) serves as a substitute for serum-free formulations. It contains purified factors required for in vitro growth and differentiation studies. The addition of supplements to media will vary, depending on the cell type being studied and the basal medium employed. It is a general cell supplement designed for use in non-complex media (e.g., minimum essential medium (MEM), Roswell Park Memorial Institute Medium (RPMI-1640)) and complex media (e.g., Ham′s F-12, Dulbecco′s Modified Eagle Medium (DME) /F-12, MEM) with sodium pyruvate.
Anwendung
Biochem./physiol. Wirkung
- Insulin: a polypeptide hormone that promotes the uptake of glucose and amino acids and may owe an observed mitogenic effect to this property.[4]
- Transferrin: an iron-transport protein. Iron is an essential trace element but can be toxic in its free form. To nourish cells in culture, iron is supplied bound to transferrin in serum.[5]
- Selenium: an essential trace element normally provided by serum.[6]
- Ethanolamine: plays a significant role in the proliferation of hybridoma cells and frequently is added to supplements used for culturing these cells.[7]
Komponenten
Contains 1.0mg/ml recombinant human insulin, 0.55mg/ml human transferrin (substantially iron-free), 0.5μg/ml sodium selenite and 0.2mg/ml ethanolamine at the 100x concentration.
Angaben zur Herstellung
Prepared in Earle′s Balanced Salt Solution (EBSS) without phenol red.
Lagerklassenschlüssel
12 - Non Combustible Liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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H Murakami et al.
Proceedings of the National Academy of Sciences of the United States of America, 79(4), 1158-1162 (1982-02-01)
A serum-free medium supplemented with a few growth factors was devised to grow lymphocyte hybridomas. The medium was developed with the hybridoma line MPC11-BL, a fusion product between a mouse plasmacytoma cell line (MPC11TG70na3) and mouse (BALB/c) spleen cells. In
Lixin Zhu et al.
American journal of physiology. Cell physiology, 295(1), C192-C202 (2008-05-16)
In a comparison of three different tissues, the membrane cytoskeleton linker protein ezrin was found to assume high levels of phosphorylation on threonine-567 (T567) in the brush border membranes of renal proximal tubule cells and small intestine enterocytes, in contrast
Mostafa Bakhti et al.
Molecular metabolism, 30, 16-29 (2019-11-27)
Translation of basic research from bench-to-bedside relies on a better understanding of similarities and differences between mouse and human cell biology, tissue formation, and organogenesis. Thus, establishing ex vivo modeling systems of mouse and human pancreas development will help not only
Rawan Eid et al.
Biochimica et biophysica acta. Molecular cell research, 1864(2), 399-430 (2016-12-13)
Iron is an essential micronutrient that is problematic for biological systems since it is toxic as it generates free radicals by interconverting between ferrous (Fe2+) and ferric (Fe3+) forms. Additionally, even though iron is abundant, it is largely insoluble so
Lixin Zhu et al.
American journal of physiology. Cell physiology, 293(3), C874-C884 (2007-06-08)
In its dormant state, the membrane cytoskeletal linker protein ezrin takes on a NH(2) terminal-to-COOH terminal (N-C) binding conformation. In vitro evidence suggests that eliminating the N-C binding conformation by Thr(567) phosphorylation leads to ezrin activation. Here, we found for
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