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2 aminoadipicacid

Manufactured by Merck Group
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Sourced in Spain

2-Aminoadipic acid is a chemical compound used in laboratory settings. It serves as a precursor for the synthesis of various organic compounds and is utilized in biochemical research. The core function of 2-Aminoadipic acid is to provide a building block for the development of other substances without further interpretation or extrapolation on its intended use.

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Lab products found in correlation

Phenylalanine, by Merck Group (1 mentions) Glutamic acid, by Merck Group (1 mentions) Selenomethionine, by Merck Group (1 mentions) Tryptophan, by Merck Group (1 mentions) Milli q purification system, by Merck Group (1 mentions) Ammonium hydroxide, by Merck Group (1 mentions) Sodium hydroxide (naoh), by Merck Group (1 mentions) Acetic acid, by Merck Group (1 mentions) Lithium carbonate, by Merck Group (1 mentions) Sodium tetraborate, by Merck Group (1 mentions) 9 fluorenylmethoxycarbonyl chloride fmoc cl, by Merck Group (1 mentions) Aicar, by Merck Group (1 mentions) Fugene 6 transfection reagent, by Promega (1 mentions) Rnaimax, by Thermo Fisher Scientific (1 mentions) Hexanoic acid, by Merck Group (1 mentions)

2 protocols using 2 aminoadipicacid

1

Amino Acid Analysis Protocol

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All
reagents employed were of analytical
grade. Sodium tetraborate, lithium carbonate, (+)-FLEC (18 mM in acetonitrile),
9-fluorenylmethoxycarbonyl chloride (FMOC-Cl), ammonium hydroxide
(28%, w/v), acetic acid, and sodium hydroxide were purchased from
Sigma-Aldrich (St. Louis, MO). Potassium carbonate was obtained from
Acros Organics (New Jersey). Acetonitrile (ACN) was supplied by Fluka
(Steinheim, Germany). Water was deionized and purified with a Milli-Q
purification system (Millipore, Belford, NJ).
DL- and L-forms
of tyrosine (Tyr), alanine (Ala), valine (Val), phenylalanine (Phe),
tryptophan (Trp), histidine (His), arginine (Arg), lysine (Lys), isoleucine
(Ile), methionine (Met), leucine (Leu), asparagine (Asn), serine (Ser),
glutamic acid (Glu), proline (Pro), threonine (Thr), 2-Aminoadipic
acid (Aad), and selenomethionine (SeMet), and D-glutamine (D-Gln),
L-glutamine (L-Gln), D-pipecolic acid (D-Pipe), D-ornithine (D-Orn),
and glycine (Gly) were purchased from Sigma-Aldrich (Madrid, Spain),
whereas D-citrulline (D-Cit), L-citrulline (L-Cit), L-pipecolic acid
(L-Pipe), and L-ornithine (L-Orn) were obtained from Fluka (Buchs,
Switzerland).
Pérez-Míguez R., Bruyneel B., Castro-Puyana M., Marina M.L., Somsen G.W, & Domínguez-Vega E. (2019). Chiral Discrimination of DL-Amino Acids by Trapped Ion Mobility Spectrometry after Derivatization with (+)-1-(9-Fluorenyl)ethyl Chloroformate. Analytical Chemistry, 91(5), 3277-3285.
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2

Preparation of Lipids, Proteins, and Cellular Components

Cited 1 time
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NAD, NADH, AICAR, hexanoic acid, octanoic acid, octanal, betaine aldehyde, betaine, and 2-aminoadipic acid were obtained (Sigma). Cholesterol, sphingomyelin, DOPC, DOPE, DOPS, and phosphatidic acid (PA) were obtained (Avanti). Alexa 546-conjugated transferrin (Tf), Alexa 555-conjugated forms of EGF, dextran, and CT were also obtained (Invitrogen). Fugene 6 Transfection Reagent was from Promega. RNAiMax was from Invitrogen. Preparations of coatomer, ARF1, ARFGAP1, BARS, Golgi membrane, and cytosol have been described14 (link),16 (link). To generate recombinant ALDH7A1, the human cDNA was expressed in bacteria (BL21) using the pET-15b vector (Novagen), followed by isolation of the 6×-his tagged form of ALDH7A1 using a nickel column. AMPK was purified from cells by transfection of a flag-tagged construct into HeLa cells, followed by immunoprecipitation of the tagged construct from cell lysates using an anti-flag antibody (M2).
Yang J.S., Hsu J.W., Park S.Y., Lee S.Y., Li J., Bai M., Alves C., Tseng W., Michelet X., Ho I.C, & Hsu V.W. (2019). ALDH7A1 inhibits the intracellular transport pathways during hypoxia and starvation to promote cellular energy homeostasis. Nature Communications, 10, 4068.
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