L-Glutamin (200 mM)
L-Glutamin (200 mM)
Gibco™

L-Glutamin (200 mM)

L-Glutamin ist eine für Zellkulturen erforderliche Aminosäure. L-Glutamin ist an der Bildung von Purin- und Pyrimidin-Nukleotiden, Aminozuckern, Glutathion, L-Glutamat undWeitere Informationen
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KatalognummerMenge
2503014920 mL
25030081100 ml
Katalognummer 25030149
Preis (EUR)
17,65
Exklusiv online
19,30
Ersparnis 1,65 (9%)
Each
Zum Warenkorb hinzufügen
Menge:
20 mL
Customize this product
Preis (EUR)
17,65
Exklusiv online
19,30
Ersparnis 1,65 (9%)
Each
Zum Warenkorb hinzufügen
L-Glutamin ist eine für Zellkulturen erforderliche Aminosäure. L-Glutamin ist an der Bildung von Purin- und Pyrimidin-Nukleotiden, Aminozuckern, Glutathion, L-Glutamat und anderen Aminosäuren sowie an der Protein-Synthese und Glukose-Produktion beteiligt. Im Gegensatz zu den meisten anderen Aminosäuren ist L-Glutamin in der Lösung nicht stabil. Die Geschwindigkeit des Abbaus verläuft in Abhängigkeit von Zeit, Temperatur und pH-Wert. Gibco™ L-Glutamin ist eine gebrauchsfertige, als Zellkulturergänzung fungierende 200 mM-Stammlösung. Die optimale Konzentration hängt von der Zellart und dem für die Zellkultur verwendeten Medium ab, liegt aber im Allgemeinen im Bereich von 2 – 6 mM.

Darüber hinaus bieten wir Gibco™ GlutaMAX™ Supplement als stabile Alternative zu L-Glutamin an.

cGMP-konformes Herstellungs- und Qualitätssystem an zwei Standorten
Gibco™ L-Glutamin wird in einer cGMP-konformen Einrichtung in Paisley, Schottland, Großbritannien, hergestellt. Die Einrichtung ist von der US-Arzneimittelbehörde FDA als Hersteller von Medizinprodukten zugelassen und nach ISO 13485-zertifiziert. Um die lückenlose Verfügbarkeit sicherzustellen, bieten wir auch ein identisches Gibco™ L-Glutamin-Produkt an, das an unserem Standort in Grand Island (25030-081) hergestellt wird. Diese Einrichtung ist von der US-Arzneimittelbehörde FDA als Hersteller von Medizinprodukten zugelassen und nach ISO 13485-zertifiziert.
Specifications
Chemischer Name oder MaterialGlutamin
Concentration or Composition (by Analyte or Components)100 X
Physikalische FormFlüssig
Empfohlene LagerungLagerbedingungen: -5 bis -20 °C. Vor Licht schützen.
Versandbedingungen: Gefrorenbei
Haltbarkeit: 24 Monate ab Herstellungsdatum
Haltbarkeit24 Monate
VersandbedingungTrockeneis
Menge20 mL
pH5 bis 6
Unit SizeEach

Häufig gestellte Fragen (FAQ)

Why did my 200 mM L-Glutamine precipitate out of solution when I thawed it?

When L-glutamine is in a concentrated stock solution it easily precipitates when cooled. Warming the solution briefly in a 37C water bath with gentle swirling will dissolve the precipitate. Do not use the product unless the precipitate is fully dissolved.

Find additional tips, troubleshooting help, and resources within our Cell Culture Support Center.

My order of L-Glutamine (Cat. No. 25030081) arrived frozen. Is it stable?

If L-Glutamine is completely or partially frozen, it is still stable. It becomes unstable when stored for extended periods of time completely thawed, especially above 2-8 degrees C.

Find additional tips, troubleshooting help, and resources within our Cell Culture Support Center.

What is your recommended method for thawing L-Glutamine before adding to cell culture media?

We recommend thawing at 2-8 degrees C and then warming at 37 degrees C until the material goes into solution. Mix it as it warms up to spend minimal time at elevated temperatures before you aliquot it.

Find additional tips, troubleshooting help, and resources within our Cell Culture Support Center.

Why did my 200 mM L-glutamine precipitate when I thawed it?

When L-glutamine is in a concentrated stock solution it easily precipitates when cooled. Warming the solution briefly in a 37 degrees C water bath with gentle swirling will dissolve the precipitate. Do not use the product unless the precipitate is fully dissolved.

Find additional tips, troubleshooting help, and resources within our Cell Culture Support Center.

Zitierungen und Referenzen (14)

Zitierungen und Referenzen
Abstract
Metabolism of 4 beta -hydroxycholesterol in humans.
Authors: Bodin Karl; Andersson Ulla; Rystedt Eva; Ellis Ewa; Norlin Maria; Pikuleva Irina; Eggertsen Gösta; Björkhem Ingemar; Diczfalusy Ulf;
Journal:J Biol Chem
PubMed ID:12077124
'One of the major oxysterols in the human circulation is 4 beta-hydroxycholesterol formed from cholesterol by the drug-metabolizing enzyme cytochrome P450 3A4. Deuterium-labeled 4 beta-hydroxycholesterol was injected into two healthy volunteers, and the apparent half-life was found to be 64 and 60 h, respectively. We have determined earlier the half-lives ... More
Activation of retinoic acid receptor-dependent transcription by all-trans-retinoic acid metabolites and isomers.
Authors: Idres Nadia; Marill Julie; Flexor Maria A; Chabot Guy G;
Journal:J Biol Chem
PubMed ID:12070176
'We have shown that four metabolites of all-trans-retinoic acid (ATRA) (4-oxo-, 4-OH-, 18-OH-, and 5,6-epoxy-RA) can induce maturation of NB4 promyelocytic leukemia cells (Idres, N., Benoit, G., Flexor, M. A., Lanotte, M., and Chabot, G. G. (2001) Cancer Res. 61, 700-705). To better understand the mechanism of action of ATRA ... More
Inhibition of transforming growth factor beta signaling and Smad-dependent activation of transcription by the Latent Membrane Protein 1 of Epstein-Barr virus.
Authors: Prokova Vassiliki; Mosialos George; Kardassis Dimitris;
Journal:J Biol Chem
PubMed ID:11781310
'Inhibition of transforming growth factor beta (TGFbeta) signaling by the Epstein-Barr virus Latent Membrane Protein 1 (LMP1) may account, at least in part, for the oncogenic activity of LMP1. We found that LMP1 is a potent inhibitor of TGFbeta signaling and Smad-dependent activation of transcription in 293 epithelial cells and ... More
Interaction codes within the family of mammalian Phox and Bem1p domain-containing proteins.
Authors:Lamark T, Perander M, Outzen H, Kristiansen K, Øvervatn A, Michaelsen E, Bjørkøy G, Johansen T,
Journal:J Biol Chem
PubMed ID:12813044
'The Phox and Bem1p (PB1) domain constitutes a recently recognized protein-protein interaction domain found in the atypical protein kinase C (aPKC) isoenzymes, lambda/iota- and zeta PKC; members of mitogen-activated protein kinase (MAPK) modules like MEK5, MEKK2, and MEKK3; and in several scaffold proteins involved in cellular signaling. Among the last ... More
Molecular rearrangements of the extracellular vestibule in NMDAR channels during gating.
Authors: Sobolevsky Alexander I; Beck Christine; Wollmuth Lonnie P;
Journal:Neuron
PubMed ID:11779481
Many N-methyl-D-aspartate receptor (NMDAR) channel blockers that have therapeutic potential can be trapped in the closed state. Using a combination of the substituted cysteine accessibility method and open channel blockers, we found that the M3 segment forms the core of the extracellular vestibule, including a deep site for trapping blockers. ... More