D2902
DMEM - low glucose
With ʟ-glutamine and sodium pyruvate, without sodium bicarbonate and phenol red, powder, suitable for cell culture
Synonym(s):
DME, Dulbecco′s Modified Eagle′s Medium - high glucose, DMEM
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About This Item
Product Name
Dulbecco′s Modified Eagle′s Medium - low glucose, With 1000 mg/L glucose and L-glutamine, without sodium bicarbonate and phenol red, powder, suitable for cell culture
form
powder
technique(s)
cell culture | mammalian: suitable
solubility
H2O: soluble 10 g/L, clear
components
glucose: low
NaHCO3: no
phenol red: no
HEPES: no
L-glutamine: yes
sodium pyruvate: yes
shipped in
ambient
storage temp.
2-8°C
Application
Dulbecco′s Modified Eagle′s Medium - low glucose is used in cell line culture (used in medium for the growth of cells) and for their maintenance. It is also used for tissue culture.
Preparation Note
Formulated to contain 10.0 grams of powder per liter of medium.
Supplement with 3.7 g/L sodium bicarbonate.
Other Notes
Investigators who work with stem cells or cell clones frequently prefer media without phenol red.
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signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Sens. 1
Storage Class
11 - Combustible Solids
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Michael D Paul et al.
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Receptor tyrosine kinases (RTKs) are single-pass membrane proteins that control vital cell processes such as cell growth, survival, and differentiation. There is a growing body of evidence that RTKs from different subfamilies can interact and that these diverse interactions can
P C Zamecnik et al.
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The tridecamer d(A-A-T-G-G-T-A-A-A-A-T-G-G), which is complementary to 13 nucleotides of the 3'- and 5'-reiterated terminal sequences of Rous sarcoma virus 35S RNA, was added to chick embryo fibroblast tissue cultures infected with Rous sarcoma virus. Inhibition of virus production resulted.
Cooperative interactions between VEGFR2 extracellular Ig-like subdomains ensure VEGFR2 dimerization.
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Prior studies have suggested that the interactions occurring between VEGFR2 extracellular domains in the absence of ligand are complex. Here we seek novel insights into these interactions, and into the role of the different Ig-like domains (D1 through D7) in