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Merck
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Key Documents

SAB1306079

Sigma-Aldrich

ANTI-V5 TAG antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

Tag from influenza hemagglutinin protein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.43

biological source

rabbit

Quality Level

100

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

technique(s)

western blot: 1:1000

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Application

ANTI-V5 TAG antibody produced in rabbit has been used in western blotting(1:1000).

Physical form

Supplied in PBS with 0.09% (W/V) sodium azide

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Stefan Bartl et al.
Neurobiology of disease, 141, 104943-104943 (2020-05-15)
Huntington's disease (HD) is caused by a highly polymorphic CAG trinucleotide expansion in the gene encoding for the huntingtin protein (HTT). The resulting mutant huntingtin protein (mutHTT) is ubiquitously expressed but also exhibits the ability to propagate from cell-to-cell to
Cory A Ocasio et al.
Nature biotechnology (2024-01-09)
The 23 human zinc finger Asp-His-His-Cys motif-containing (ZDHHC) S-acyltransferases catalyze long-chain S-acylation at cysteine residues across an extensive network of hundreds of proteins important for normal physiology or dysregulated in disease. Here we present a technology to directly map the
Gonzalo Federico Mayol et al.
Biochimica et biophysica acta. Molecular cell research, 1867(1), 118566-118566 (2019-11-02)
Nuclear-cytoplasmic trafficking of proteins is a highly regulated process that modulates multiple biological processes in eukaryotic cells. In Giardia lamblia, shuttling has been described from the cytoplasm to nuclei of proteins during the biological cell cycle of the parasite. This

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