assay
≥95% (HPLC)
form
lyophilized
composition
Peptide Content, ≥68%
storage condition
protect from light
storage temp.
−20°C
Application
The octapeptide YGAVVNDL is closely related to the nonapeptide YAGAVVNDL used to inhibit herpes virus ribonucleotide reductase.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
A Marcello et al.
Journal of chemotherapy (Florence, Italy), 7(5), 403-405 (1995-10-01)
Peptides capable of selectively disrupting protein-protein interactions that are required for viral replication represent potential agents for antiviral therapy. The first example of viral product that could be inhibited by the peptide YAGAVVNDL, targeted to the functional interaction between subunits
J Furlong et al.
Virology, 182(2), 846-851 (1991-06-01)
The open reading frame of the large subunit (R1) of herpes simplex virus type 1 (HSV-1) ribonucleotide reductase has been positioned downstream of the phage T7 gene 10 promoter in the expression vector, pET. Transformation of this recombinant plasmid into
E Telford et al.
The Journal of general virology, 71 ( Pt 6), 1373-1378 (1990-06-01)
The synthetic nonapeptide YAGAVVNDL [identical to the nine carboxy-terminal amino acids of the small subunit of herpes simplex virus (HSV)-encoded ribonucleotide reductase (RR)] was found to inhibit the RR activity induced by equine herpesvirus type 1 subtype 1 (EHV-1). Parallel
A Marcello et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(19), 8994-8998 (1994-09-13)
Mimetic peptides capable of selectively disrupting protein-protein interactions represent potential therapeutic agents for inhibition of viral and cellular enzymes. This approach was first suggested by the observation that the peptide YAGAVVNDL, corresponding to the carboxyl-terminal 9 amino acids of the
H Paradis et al.
The Journal of biological chemistry, 263(31), 16045-16050 (1988-11-05)
Herpes simplex virus (HSV) ribonucleotide reductase activity is specifically inhibited by a synthetic peptide, Tyr-Ala-Gly-Ala-Val-Val-Asn-Asp-Leu (HSV H2-(7-15], corresponding to the carboxyl terminus of its subunit 2 (H2). In order to elucidate the mechanism of action of the nonapeptide a photoreactive
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