MAB10209-I

Anti-HSV-2 Nucleocapsid p40 Antibody, clone 3E1

• UNSPSC Code: 12352203
• NACRES: NA.41

Properties

• biological source: mouse
• Quality Level: 200
• conjugate: unconjugated
• antibody form: purified antibody
• antibody product type: primary antibodies
• clone: 3E1, monoclonal
• mol wt: calculated mol wt 66.94 kDa
• purified by: using protein G
• species reactivity: virus
• packaging: antibody small pack of 100 μL
• technique(s): immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
• isotype: IgG1
• epitope sequence: Unknown
• UniProt accession no.: P89449
• shipped in: 2-8°C
• target post-translational modification: unmodified

Description

General description

Capsid scaffolding protein (UniProt: P89449; also known as Capsid protein P40, Nucleocapsid protein P40, Protease precursor, pPR, Virion structural protein UL26) is encoded by the UL26 gene (Gene ID: 1487310) in Herpes Simplex virus 2 (HSV-2). HSV-2 is a large complex DNA-containing virus that is shown to induce the synthesis of at least 50 new polypeptides in infected cells. It replicates in the nuclei of mammalian cells. Its nuclear localization signal is localized in amino acids 428-431. Following its synthesis, Capsid protein 40 is processed into Assemblin (aa 1-237), and Assembly protein (aa 248-637) by proteolytic cleavage. Assemblin is a protease that plays an essential role in virion assembly within the nucleus. It exists in a monomer-dimer equilibrium with the dimer being the active species. It catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The assembly protein is involved in capsid assembly. It acts as a scaffold protein by binding major capsid protein and multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. It is cleaved by Assemblin after capsid completion and the cleavages products are evicted from the capsid before or during DNA packaging. HSV is reported to evade the immune system through interference with MHC class I antigen presentation on the cell surface, by blocking the transporter associated with antigen processing (TAP) induced by the secretion of infected cell protein 47 (ICP-47) by HSV. ICP-47 prevents initiation of a CTL-response against HSV, allowing the virus to survive for a protracted period in the host. (Ref.: Goldsmith, K., et a. (1998). J. Exp. Med. 187(3); 341-348; Heilman, CJ., et al. (1981). J. Virol. 40(2); 508-515).

Specificity

Clone 3E1 is a mouse monoclonal antibody that detects nucleocapsid protein p40 in Herpes Simplex virus 2

Immunogen

Purified HSV-2 nucleocapsids.

Application

Quality Control Testing

Evaluated by Immunohistochemistry (Paraffin) in HSV-2-positive tissue sections.

Immunohistochemistry (Paraffin) Analysis: A 1:50 dilution of this antibody detected HSV-2 Nucleocapsid p40 in HSV-2-positive tissue sections.

Anti-HSV-2 Nucleocapsid p40, clone 3E1, Cat. No. MAB10209-I, is a mouse monoclonal antibody that detects HSV-2 Nucleocapsid p40 and is tested for use in Immunohistochemistry (Paraffin).

Physical form

Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Recommend storage at +2°C to +8°C. For long term storage antibodies can be kept at -20°C. Avoid repeated freeze-thaws.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Safety Information

• Storage Class: 12 - Non Combustible Liquids
• wgk_germany: WGK 1
• flash_point_f: Not applicable
• flash_point_c: Not applicable