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A propos de cet article
Formule empirique (notation de Hill) :
C4H7NO5
Numéro CAS:
Poids moléculaire :
149.10
PubChem Substance ID:
eCl@ss:
32160406
UNSPSC Code:
12352106
NACRES:
NA.32
EC Number:
224-299-4
MDL number:
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YYLQUHNPNCGKJQ-JCYAYHJZSA-N
InChI
1S/C4H7NO5/c5-1(3(7)8)2(6)4(9)10/h1-2,6H,5H2,(H,7,8)(H,9,10)/t1-,2-/m1/s1
SMILES string
N[C@H]([C@@H](O)C(O)=O)C(O)=O
storage temp.
−20°C
Quality Level
Gene Information
human ... GLUL(2752)
mouse ... GLUL(14645)
General description
DL-threo-β-hydroxyaspartic acid (THA) is a glutamate uptake inhibitor.
Application
DL-threo-β-Hydroxyaspartic acid (THA) has been used to block glutamate transport in cannulated sprague dawley rat.
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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A Hirata et al.
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Erythropoietin (EPO) is a chemokine hormone that is widely distributed throughout the body including nervous system. For last years its role as cytokine involved in many physiological processes out of the bone marrow has been suggested. Moreover, it plays a
Nina Bionda et al.
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A simple and practical general synthetic protocol towards orthogonally protected tHyAsp derivatives fully compatible with Fmoc solid-phase peptide synthetic methodology is reported. Our approach includes enantioresolution of commercially available D: ,L: -tHyAsp racemic mixture by co-crystallization with L: -Lys, followed
Jixu Yu et al.
Brain research, 1257, 102-107 (2009-01-13)
Threohydroxyaspartate (THA)-induced glutamate excitotoxicity in organotypic culture of rat spinal cord is a well-known model of motor neuron degeneration. THA causes accumulation of synaptic glutamate and over stimulation of the postsynaptic receptor by inhibiting glutamate uptake. This model has also
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Methods in molecular biology (Clifton, N.J.), 446, 85-94 (2008-04-01)
Vitamin K-dependent coagulation plasma proteins possess from 9-12 residues of gamma-carboxyglutamic acid (Gla) distributed over a ca. 45 amino acid peptide sequence, i.e., the Gla domain, which encompasses the NH2-terminal region. In addition, epidermal growth factor (EGF) homology units present
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