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H6030

Sigma-Aldrich

Anti-HSV antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(e):

Anti-Herpes Simplex Virus

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About This Item

MDL-Nummer:
MFCD02263028
UNSPSC-Code:
12352203
NACRES:
NA.56

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Methode(n)

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

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

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Allgemeine Beschreibung

Recognizes N- and C-terminal HSV fusion proteins.

Immunogen

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

Anwendung

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)

Biochem./physiol. Wirkung

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.

Physikalische Form

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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Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°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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