This product is tested for solubility at 50 mg/mL in 1 M NaOH. The solubility in water has not been determined.
C6154
Z-Gln-Gly
γ-glutamyl donor substrate
Synonym(s):
N2-[(phenylmethoxy)carbonyl]-L-glutaminyl-glycine
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1 G
$215.00
About This Item
Empirical Formula (Hill Notation):
C15H19N3O6
CAS Number:
Molecular Weight:
337.33
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
Recommended Products
Quality Level
form
powder
storage temp.
−20°C
SMILES string
NC(=O)CCC(NC(=O)OCc1ccccc1)C(=O)NCC(O)=O
InChI
1S/C15H19N3O6/c16-12(19)7-6-11(14(22)17-8-13(20)21)18-15(23)24-9-10-4-2-1-3-5-10/h1-5,11H,6-9H2,(H2,16,19)(H,17,22)(H,18,23)(H,20,21)
InChI key
SOUXAAOTONMPRY-UHFFFAOYSA-N
Amino Acid Sequence
Z-Gln-Gly
Application
Biochem/physiol Actions
N-Benzyloxycarbonyl-L-Glutaminylglycine (Z-Gln-Gly, Z-QG) is used as a substrate to differentiate and characterize transglutaminase(s) (TGase) that catalyzes the post-translational covalent cross-linking of Gln- and Lys-containing peptides. Z-QG supports glutamyl-level cross-linking applications thruough surface modification.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Syeda Warisul Fatima et al.
Bioresource technology, 287, 121391-121391 (2019-05-12)
This work studied the production of Transglutaminase (TGase) using wheat bran as carbon source. The medium components and culture conditions were optimized by statistical Box-Behnken response surface methodology. The release of active Transglutaminase was enhanced by adding (i) protease to
Momoko Kitaoka et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 17(19), 5387-5392 (2011-04-07)
A new synthetic strategy for DNA-enzyme conjugates with a novel architecture was explored using a natural cross-linking catalyst, microbial transglutaminase (MTG). A glutamine-donor substrate peptide of MTG was introduced at the 5-position on the pyrimidine of deoxyuridine triphosphate to prepare
Kyunga Sung et al.
Biotechnology journal, 5(5), 456-462 (2010-03-12)
A chemically modified glass surface displaying a glutamyl donor substrate peptide (Z-QG) was developed for microbial transglutaminase (MTG)-mediated immobilization of recombinant proteins tagged with an MTG-reactive lysine-containing substrate peptide (K-tag). To evaluate the surface modification conditions affecting the enzymatic protein
Dongdong Mu et al.
Applied microbiology and biotechnology, 102(13), 5533-5543 (2018-04-25)
Microbial transglutaminase (MTG) from Streptomyces mobaraensis has been widely used for crosslinking proteins in order to acquire products with improved properties. To improve the yield and enable a facile and efficient purification process, recombinant vectors, harboring various heterologous signal peptide-encoding
D Ramos et al.
The Journal of organic chemistry, 66(9), 2948-2956 (2001-04-28)
A novel methodology for the enzymatic preparation from suitably derivatized oligosaccharides of N-linked neoglycopeptides using the microbial glutaminyl-peptide gamma-glutamyl transferase, transglutaminase (TGase), is described. N-Allyl glycosides of various oligosaccharides were photochemically coupled with cysteamine to yield amino-terminated thioether spacers, which
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