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H6030

Sigma-Aldrich

Anti-HSV antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

Anti-Herpes Simplex Virus

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About This Item

Número MDL:
MFCD02263028
Código UNSPSC:
12352203
NACRES:
NA.56

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

técnica(s)

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

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

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Descrição geral

Recognizes N- and C-terminal HSV fusion proteins.

Imunogênio

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

Aplicação

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)

Ações bioquímicas/fisiológicas

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.

forma física

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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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

nwg

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

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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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