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G7513

Sigma-Aldrich

L-Glutamine solution

200 mM, solution, sterile-filtered, BioXtra, suitable for cell culture

Synonym(s):

Glavamin, Levoglutamide

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.75

sterility

sterile-filtered

Quality Level

300
400

product line

BioXtra

form

solution

concentration

200 mM

technique(s)

cell culture | mammalian: suitable

impurities

endotoxin, tested

shipped in

dry ice

storage temp.

−20°C

SMILES string

N[C@@H](CCC(N)=O)C(O)=O

InChI

1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1

InChI key

ZDXPYRJPNDTMRX-VKHMYHEASA-N

Gene Information

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General description

L-glutamine is an essential amino acid that is a crucial component of culture media that serves as a major energy source for cells in culture. L-glutamine is very stable as a dry powder and as a frozen solution. In liquid media or stock solutions, however, L-glutamine degrades relatively rapidly. Optimal cell performance usually requires supplementation of the media with L-glutamine prior to use.

Application

L-glutamine is an essential amino acid that is a crucial component of culture media, which serves as a major energy source for cells in culture. Optimal cell performance usually requires supplementation of the medium with L-glutamine prior to use.

Preparation Note

Prepared in cell culture grade water.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Oncotarget, 8(1), 757-768 (2016-10-22)
The newly discovered short (9 amino acid) non-RGD S-S bridged cyclic peptide ALOS-4 (H-cycl(Cys-Ser-Ser-Ala-Gly-Ser-Leu-Phe-Cys)-OH), which binds to integrin αvβ3 is investigated as peptide carrier for targeted drug delivery against human metastatic melanoma. ALOS4 binds specifically the αvβ3 overexpressing human metastatic
Miguel Pérez-Garrastachu et al.
Nucleus (Austin, Tex.), 8(5), 515-533 (2017-07-12)
Nucleoporins are the main components of the nuclear-pore complex (NPC) and were initially considered as mere structural elements embedded in the nuclear envelope, being responsible for nucleocytoplasmic transport. Nevertheless, several recent scientific reports have revealed that some nucleoporins participate in
Ofir Cohn et al.
Scientific reports, 6, 37115-37115 (2016-11-16)
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