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50370

Gly-Phe

Name: Gly-Phe
Brand: SIAL

puriss., ≥99.0% (NT)

Synonym(s):

Glycyl-L-phenylalanine

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About This Item

Linear Formula:

NH₂CH₂CONHCH(COOH)CH₂C₆H₅

CAS Number:

3321-03-7

Molecular Weight:

222.24

EC Number:

222-027-9

UNSPSC Code:

12352200

PubChem Substance ID:

329757592

Beilstein/REAXYS Number:

2279318

MDL number:

MFCD00065110

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grade

puriss.

assay

≥99.0% (NT)

form

crystalline

optical activity

[α]20/D +42±2°, c = 2% in H₂O

color

white

mp

~264 °C (dec.)

application(s)

peptide synthesis

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

Storage Class

13 - Non 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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Resolution of chiral compounds by HPLC using mobile phase additives and a porous graphitic carbon stationary phase.

B J Clark et al.

Journal of pharmaceutical and biomedical analysis, 7(12), 1883-1888 (1989-01-01)

The cyanogenic substrate for horseradish peroxidase is a conjugated enamine.

D J Porter et al.

The Journal of biological chemistry, 262(19), 9154-9159 (1987-07-05)

We identify the cyanogenic substrate for horseradish peroxidase (HRP) as a conjugated enamine and explore this unusual reaction using alpha-aminocinnamate (RH) as follows. 1) HRP catalyzes the oxidation of RH by O2 (and its peroxidation by H2O2 to form R-R)

Tresyl-mediated synthesis: kinetics of competing coupling and hydrolysis reactions as a function of pH, temperature, and steric factors.

J J Sperinde et al.

Bioconjugate chemistry, 10(2), 213-220 (1999-03-17)

Kinetic parameters have been measured for coupled nucleophilic and solvolytic reactions of 2,2,2-trifluoroethanesulfonyl (tresyl)-modified poly(ethylene glycol) based on a system of coupled differential equations implied by recently proposed elementary reaction mechanisms. Fitted kinetic parameters were found to be strong functions

Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport.

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

Improvement in performance of affinity gels containing Gly-D-Phe as a ligand to thermolysin due to increasing the spacer chain length.

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

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