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SRP2121

Sigma-Aldrich

VP16 (411-490), GST tagged from human herpesvirus 2

recombinant, expressed in E. coli, ≥80% (SDS-PAGE)

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.26

biological source

human

recombinant

expressed in E. coli

assay

≥80% (SDS-PAGE)

form

frozen liquid

mol wt

~36 kDa

packaging

pkg of 10 μg
pkg of 50 μg

storage condition

avoid repeated freeze/thaw cycles

concentration

450 μg/mL

color

clear colorless

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... UL48(1487335)

General description

Herpes virus VP16 is a 65kDa phosphoprotein. In the viral replication cycle, the protein is expressed at a late stage.[1][2]

Biochem/physiol Actions

Herpes virus VP16 activates expression of immediate early genes in virally-infected cells. As most other eukaryotic transcriptional activator proteins, VP16 has a modular domain structure: its N-terminus is involved in DNA-protein interactions, while its C-terminal 79 amino acids have proven to be an especially potent transactivation domain. VP16 has been shown to bind to TBP, TFIIB, and replication factor A.
The protein activates the lytic cycle of the virus. It has been shown to have a role in viral assembly and maturation.[1]

Physical form

Clear and colorless frozen liquid solution

Preparation Note

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Role of the TATA Binding Protein?Transcription Factor IIB Interaction in Supporting Basal and Activated Transcription in Plant Cells
Songqin Pan
Plant Cell, 12(1), 125-136 (2000)
De Novo Synthesis of VP16 Coordinates the Exit from HSV Latency In Vivo
Richard L. Thompson
PLoS ONE (2009)
Evidence that Herpes Simplex Virus VP16 Is Required for Viral Egress Downstream of the Initial Envelopment Event
Karen L. Mossman
Journal of Virology, 74(14), 6287-6299 (2000)
K F Stringer et al.
Nature, 345(6278), 783-786 (1990-06-28)
The potent transactivation domain of the herpes simplex virion protein VP16 was used as a column ligand for affinity chromatography. VP16 binds strongly and highly selectively to the human and yeast TATA box-binding factors. Our results imply that the principal
L E Post et al.
Cell, 24(2), 555-565 (1981-05-01)
We report a system for investigating promoters of eucaryotic cell and virus genes based on analyses of the regulation of herpes simplex virus 1 (HSV-1) thymidine kinases whose structural gene sequences have been fused to the promoter of the gene

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