G5136
γ-Glu-ε-Lys
≥98.0% (TLC)
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About This Item
Produits recommandés
Nom du produit
γ-Glu-ε-Lys,
Essai
≥98.0% (TLC)
Niveau de qualité
Forme
powder
Couleur
white
Température de stockage
−20°C
Chaîne SMILES
NC(CCCCNC(=O)CCC(N)C(O)=O)C(O)=O
InChI
1S/C11H21N3O5/c12-7(10(16)17)3-1-2-6-14-9(15)5-4-8(13)11(18)19/h7-8H,1-6,12-13H2,(H,14,15)(H,16,17)(H,18,19)
Clé InChI
JPKNLFVGUZRHOB-UHFFFAOYSA-N
Application
GammaGlu-epsilonLys (γ-Glu-ε-Lys) is used to study the functions and processing of endo-epsilon(-gamma-Glu)-Lys isopeptide bonds in biological processes.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
Development (Cambridge, England), 136(11), 1835-1847 (2009-05-01)
Fertilization is accompanied by the construction of an extracellular matrix that protects the new zygote. In sea urchins, this structure is built from glycoproteins residing at the egg surface and in secretory vesicles at the egg cortex. Four enzymatic activities
Molecular & general genetics : MGG, 253(1-2), 20-25 (1996-11-27)
We previously detected in salivary gland secretions of the medicinal leech (Hirudo medicinalis) a novel enzymatic activity, endo-epsilon(gamma-Glu)-Lys isopeptidase, which cleaves isopeptide bonds formed by transglutaminase (Factor XIIIa) between glutamine gamma-carboxamide and the epsilon-amino group of lysine. Such isopeptide bonds
Tissue engineering, 12(6), 1467-1474 (2006-07-19)
This study investigated the effect on the mechanical and physicochemical properties of type II collagen scaffolds after cross-linking with microbial transglutaminase (mTGase). It is intended to develop a collagen-based scaffold to be used for the treatment of degenerated intervertebral discs.
Biochemistry. Biokhimiia, 66(12), 1368-1373 (2002-01-29)
Destabilase, endo-epsilon-(gamma-Glu)-Lys-isopeptidase, was prepared from the salivary gland secretion of the medicinal leech (Hirudo medicinalis). The secretion prepared by the known method of Rigbi et al. (1987) (secretion-K) lacks the destabilase-characteristic highly specific isopeptidase activity (the D-dimer-monomerizing activity) because of
Amino acids, 44(1), 129-142 (2012-03-13)
Transglutaminases catalyze the formation of γ-glutamylamines utilizing glutamyl residues and amine-bearing compounds such as lysyl residues and polyamines. These γ-glutamylamines can be released from proteins by proteases in an intact form. The free γ-glutamylamines can be catabolized to 5-oxo-L-proline and
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