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H6030

Sigma-Aldrich

Anti-HSV antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Anti-Herpes Simplex Virus

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About This Item

Numero MDL:
MFCD02263028
Codice UNSPSC:
12352203
NACRES:
NA.56

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

tecniche

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

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

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Descrizione generale

Recognizes N- and C-terminal HSV fusion proteins.

Immunogeno

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

Applicazioni

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)

Azioni biochim/fisiol

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.

Stato fisico

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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Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Certificati d'analisi (COA)

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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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