Skip to Content
Merck
All Photos(1)

Key Documents

Safety Information

SCP0167

Sigma-Aldrich

Herpes Virus Inhibitor 2

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

Empirical Formula (Hill Notation):
C38H59N9O13
Molecular Weight:
849.93
UNSPSC Code:
12352200
NACRES:
NA.32

Assay

≥95% (HPLC)

form

lyophilized

composition

Peptide Content, ≥68%

storage condition

protect from light

storage temp.

−20°C

Amino Acid Sequence

Tyr-Gly-Ala-Val-Val-Asn-Asp-Leu

Application

The octapeptide YGAVVNDL is closely related to the nonapeptide YAGAVVNDL used to inhibit herpes virus ribonucleotide reductase.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

SCP0167-5MG:

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
SC0728

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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
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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service