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H6030

Sigma-Aldrich

Anti-HSV antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-Herpes Simplex Virus

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About This Item

Numéro MDL:
MFCD02263028
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.56

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Technique(s)

immunoprecipitation (IP): 1.0 μg/mL
western blot: 2.5 μg/mL

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

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Description générale

Recognizes N- and C-terminal HSV fusion proteins.

Immunogène

synthetic peptide corresponding to amino acids 290−300 of glycoprotein-D precursor, an envelop component of herpes simplex virus.

Application

Anti-HSV antibody was used to expand the repertoire of plasmids for PCR-mediated epitope tagging in yeast.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Chromatin immunoprecipitation (1 paper)
Western Blotting (1 paper)

Actions biochimiques/physiologiques

Anti-HSV is developed in rabbits using a synthetic peptide (K-QPELAPEDPED) conjugated to KLH via the N-terminal lysine. The peptide corresponds to amino acids 290-300 of Glycoprotein D precursor which is an envelope component of herpes simplex virus. Anti-HSV antibody reacts specifically with HSV tagged fusion proteins, using immunoblotting and immunoprecipitation techniques.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Expanding the repertoire of plasmids for PCR-mediated epitope tagging in yeast
Moqtaderi Z, Struhl K
Yeast, 4, 287-292 (2008)
Obstetrical roundabout.
H E Cudby
Midwives chronicle, 91(1089), 301-301 (1978-10-01)
P O Olins et al.
Current opinion in biotechnology, 4(5), 520-525 (1993-10-01)
Recent advances in protein expression in E. coli have focused primarily on the enhancement of protein quality. Problems in mRNA translation such as inefficient initiation, mistranslation, frame-shifting and frame-hopping can often be addressed by altering heterologous gene-coding sequences. Fusion technology
Christine E Cucinotta et al.
PLoS genetics, 11(8), e1005420-e1005420 (2015-08-05)
Eukaryotes regulate gene expression and other nuclear processes through the posttranslational modification of histones. In S. cerevisiae, the mono-ubiquitylation of histone H2B on lysine 123 (H2B K123ub) affects nucleosome stability, broadly influences gene expression and other DNA-templated processes, and is
Zarmik Moqtaderi et al.
Yeast (Chichester, England), 25(4), 287-292 (2008-03-14)
Epitope tagging of yeast proteins provides a convenient means of tracking proteins of interest in Western blots and immunoprecipitation experiments without the need to raise and test specific antibodies. We have constructed four plasmids for use as templates in PCR-based

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