G2752
Gly-Phe
≥97.0% (TLC)
Synonym(s):
Glycyl-L-phenylalanine
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About This Item
Linear Formula:
NH2CH2CONHCH(COOH)CH2C6H5
CAS Number:
Molecular Weight:
222.24
Beilstein:
2279318
EC Number:
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
Recommended Products
Product Name
Gly-Phe,
Assay
≥97.0% (TLC)
Quality Level
form
crystalline
color
white
mp
264 °C
storage temp.
−20°C
SMILES string
NCC(=O)N[C@@H](Cc1ccccc1)C(O)=O
InChI
1S/C11H14N2O3/c12-7-10(14)13-9(11(15)16)6-8-4-2-1-3-5-8/h1-5,9H,6-7,12H2,(H,13,14)(H,15,16)/t9-/m0/s1
InChI key
JBCLFWXMTIKCCB-VIFPVBQESA-N
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Related Categories
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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T Takarada et al.
Chemistry (Weinheim an der Bergstrasse, Germany), 6(21), 3906-3913 (2000-12-29)
Oligopeptides are efficiently hydrolyzed by Ce(IV) to the corresponding amino acids under mild conditions. The pseudo first-order rate constants for the hydrolysis of H-Gly-Phe-OH and H-Gly-Gly-OH at pH 7.0 and 50 degrees C are 3.5 x 10(-1) and 2.8 x
Susan Weng Larsen et al.
European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 22(5), 399-408 (2004-07-22)
Oil-based depot formulations may constitute a future delivery method for small peptides. Thus, a requirement is attainment of sufficient oil solubility for such active compounds. A model dipeptide (Gly-Phe) has been converted into lipophilic prodrugs by esterification at the C-terminal
Kuniyo Inouye et al.
Bioscience, biotechnology, and biochemistry, 71(8), 2083-2086 (2007-08-11)
The aim of this study was to improve the performance of affinity gels containing glycyl-D-phenylalanine (Gly-D-Phe) as a ligand to thermolysin. Gly-D-Phe was immobilized to the resin through spacers of varying chain lengths. The resulting affinity gels had spacer chain
Roderick Y H Lim et al.
Proceedings of the National Academy of Sciences of the United States of America, 103(25), 9512-9517 (2006-06-14)
Natively unfolded phenylalanine-glycine (FG)-repeat domains are alleged to form the physical constituents of the selective barrier-gate in nuclear pore complexes during nucleocytoplasmic transport. Presently, the biophysical mechanism behind the selective gate remains speculative because of a lack of information regarding
S J Reshkin et al.
The American journal of physiology, 260(3 Pt 2), R563-R569 (1991-03-01)
The transport mechanisms for the dipeptide glycyl-L-phenylalanine (Gly-Phe) and L-phenylalanine (Phe) were characterized in fish intestinal brush-border membrane vesicles (BBMV). Gly-Phe was rapidly hydrolyzed only intravesicularly with almost total hydrolysis occurring even at 10 s. Dipeptide uptake was not stimulated
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