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

L-glutamina (200 mM)

La L-glutamina es un aminoácido necesario para el cultivo celular. La L-glutamina participa en la formación de purina y nucleótidosMás información
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Número de catálogoCantidad
2503014920 mL
25030081100 mL
2503016420 x 100 mL
Número de catálogo 25030149
Precio (CLP)
13.251
Each
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Cantidad:
20 mL
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Precio (CLP)
13.251
Each
Añadir al carro de la compra
La L-glutamina es un aminoácido necesario para el cultivo celular. La L-glutamina participa en la formación de purina y nucleótidos de pirimidina, aminoazúcares, glutatión, L-glutamato y otros aminoácidos, así como en la síntesis de proteínas y la producción de glucosa. A diferencia de la mayoría de los demás aminoácidos, la L-glutamina no es estable en solución. El ritmo al que avanza la degradación depende del tiempo, la temperatura y el pH. La L-glutamina Gibco™ es una solución madre de 200 mM lista para usar que actúa como un suplemento de cultivo celular. La concentración óptima depende del tipo de célula y del medio empleado para cultivar las células, pero por lo general se sitúa en el intervalo de 2 a 6 mm.

También ofrecemos el suplemento Gibco™ GlutaMAX™ como una alternativa estable a la L-glutamina.

Sistema de fabricación y calidad según las buenas prácticas de fabricación actuales en dos instalaciones
La L-glutamina Gibco™ se fabrica en unas instalaciones conformes con las buenas prácticas de fabricación actuales situadas en Paisley, Escocia (Reino Unido). Las instalaciones están registradas en la Agencia estadounidense de alimentos y medicamentos (FDA) como fabricante de dispositivos médicos y están certificadas según la norma ISO 13485. Para la continuidad de la cadena de suministro, ofrecemos un producto de L-glutamina Gibco™ idéntico fabricado en nuestras instalaciones de Grand Island (EE. UU.) (25030-081). Estas instalaciones se han registrado en la FDA como fabricante de dispositivos médicos y tienen la certificación según la norma ISO 13485.
Especificaciones
Nombre del producto químico o materialGlutamina
Concentration or Composition (by Analyte or Components)100 X
Forma físicaLíquido
Almacenamiento recomendadoCondiciones de almacenamiento: De – 5 a – 20 °C. Proteger de la luz
Condiciones de envío: Congelado
Vida útil: 24 meses a partir de la fecha de fabricación
Duración de almacenamiento24 meses
Condiciones de envíoHielo seco
Cantidad20 mL
pH5 to 6
Unit SizeEach

Preguntas frecuentes

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.

Citations & References (14)

Citations & References
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