H6030
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
Prodotti consigliati
Origine biologica
rabbit
Livello qualitativo
Coniugato
unconjugated
Forma dell’anticorpo
affinity isolated antibody
Tipo di anticorpo
primary antibodies
Clone
polyclonal
Stato
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)
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
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Expanding the repertoire of plasmids for PCR-mediated epitope tagging in yeast
Yeast, 4, 287-292 (2008)
Obstetrical roundabout.
Midwives chronicle, 91(1089), 301-301 (1978-10-01)
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
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
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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