MAB8672-I
Anti-HSV1-ICP8 Antibody, clone 10A3
clone 10A3, from mouse
Synonyme(s) :
Major DNA-binding protein, HSV1-ICP8, Infected cell protein 8
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About This Item
Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
mouse
Niveau de qualité
Forme d'anticorps
purified immunoglobulin
Type de produit anticorps
primary antibodies
Clone
10A3, monoclonal
Espèces réactives
virus
Réactivité de l'espèce (prédite par homologie)
all
Technique(s)
western blot: suitable
Isotype
IgG1κ
Numéro d'accès UniProt
Conditions d'expédition
ambient
Modification post-traductionnelle de la cible
unmodified
Description générale
Major DNA-binding protein (UniProt: P04296) is encoded by DBP (also known as Infected cell protein 8, ICP8, UL29) gene (Gene ID: 2703458) in human herpes simplex virus 1. HSV1-ICP8 is a 128 kDa, single stranded DNA binding protein of the herpesviridae family. It is an essential replication factor for both Herpes Simplex Virus Type 1 (HSV-1) and Adeno-Associated Virus (AAV) DNA replication. It binds tightly and cooperatively to ssDNA and destabilizes dsDNA helices, promotes DNA strand transfer, and renaturation of ssDNA. ICP8 is reported to regulate viral gene expression by repressing transcription from the parental viral genome and stimulating gene expression from the progeny genome. It is known to associate in replication compartments with over 50 cellular and viral proteins-many of which are involved in DNA replication and repair, recombination, and chromatin modeling. In the absence of DNA replication, HSV1-ICP8 is found in the nuclear framework-associated structures (pre-replicative sites); however, as viral DNA replication proceeds, it migrates to globular intranuclear structures (replication compartments). (Ref.: Glauser, D.L., et al. (2007). J. Virol. 81(9): 4732-4743; Tolun, G., et al. (2013). Nucleic Acids Res. 41(11): 5927 5937).
Spécificité
Clone 10A3 detects ICP-8 protein in human herpes simplex virus 1.
Immunogène
ICP8 purified from U-35-VERO cells.
Application
This mouse monoclonal Anti-HSV1-ICP8, clone 10A3 , Cat. No. MAB8672-I is validated for use in Western Blotting for the detection of Herpes Simplex Virus Infected cell protein 8.
Western Blotting Analysis: A representative lot detected HSV1-ICP8 in HeLa cells (Glauser, D.L., et. al. (2007). J Virol. 81(9):4732-43).
Qualité
Evaluated by Western Blotting in using recombinant protein.
Western Blotting Analysis: A 1:5,000 dilution of this antibody detected 1.25 µg of 1CB8 recombinant protein.
Western Blotting Analysis: A 1:5,000 dilution of this antibody detected 1.25 µg of 1CB8 recombinant protein.
Description de la cible
~128 kDa observed; 128.35 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Forme physique
Format: Purified
Autres remarques
Concentration: Please refer to lot specific datasheet.
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Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Certificats d'analyse (COA)
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Fumio Maeda et al.
Journal of virology, 91(12) (2017-03-31)
Upon herpes simplex virus 1 (HSV-1) infection, the CD98 heavy chain (CD98hc) is redistributed around the nuclear membrane (NM), where it promotes viral de-envelopment during the nuclear egress of nucleocapsids. In this study, we attempted to identify the factor(s) involved
Ken Sagou et al.
Journal of virology, 84(4), 2110-2121 (2009-12-04)
Herpesvirus nucleocapsids assemble in the nucleus and must cross the nuclear membrane for final assembly and maturation to form infectious progeny virions in the cytoplasm. It has been proposed that nucleocapsids enter the perinuclear space by budding through the inner
Zhuoming Liu et al.
Journal of virology, 89(17), 8982-8998 (2015-06-19)
To clarify the function(s) of the herpes simplex virus 1 (HSV-1) major virion structural protein UL47 (also designated VP13/14), we screened cells overexpressing UL47 for UL47-binding cellular proteins. Tandem affinity purification of transiently expressed UL47 coupled with mass spectrometry-based proteomics
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