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D6444

Sigma-Aldrich

Anti-DBP5 (N-terminal) antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

Anti-DDX19B, Anti-DEAD (Asp-Glu-Ala-As) box polypetide 19B, Anti-DEAD5, Anti-DED box protein 19B

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About This Item

Código UNSPSC:
12352203

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

antigen ~53 kDa

reatividade de espécies

rat (predicted), human, mouse (predicted)

concentração

~1 mg/mL

técnica(s)

immunoprecipitation (IP): 5-10 μL using HEK-293T cell lysate
indirect immunofluorescence: 2.5-5 μg/mL using paraformaldehyde-fixed HEK-293T cells over-expressing human DBP5
western blot: 1-2 μg/mL using HEK-293T cell lysate

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... DDX19B(11269)
mouse ... Ddx19b(234733)

Descrição geral

DBP5 belongs to the family of the DEAD-box helicases that are involved in cellular RNA metabolism from transcription through pre-mRNA splicing, nuclear export, translation initiation to RNA degradation. It localizes within the cytoplasm and at the nuclear rim, where it interacts with components of the nuclear pore complex (NPC). It shuttles between the nucleus and the cytoplasm by using Nup159 as a binding platform.

Aplicação

Anti-DBP5 antibody produced in rabbit is suitable for immunoprecipitation at a working amount of 5-10μL using HEK-293T cell lysate, immunoblotting at a working concentration of 1-2μg/mL using HEK-293T cell lysate and immunofluorescence at a working concentration of 2.5-5μg/mL using paraformaldehyde fixed HEK-293T cells over-expressing human DBP5.

Ações bioquímicas/fisiológicas

DBP5 is required for mRNA export from the nucleus in an ATP-dependent manner. It is also involved in translation termination, where it recognizes stop-codon by controlling eRF1-eRF3 interaction.

forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Exoneração de responsabilidade

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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Código de classe de armazenamento

12 - Non Combustible Liquids

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificados de análise (COA)

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DEAD-box proteins: the driving forces behind RNA metabolism.
Sanda Rocak et al.
Nature reviews. Molecular cell biology, 5(3), 232-241 (2004-03-03)
Edward Silverman et al.
Gene, 312, 1-16 (2003-08-12)
Members of the DExD/H-box family of RNA helicases are involved in many processes and complexes within the cell. While individual DExD/H helicase family members have been studied extensively, the mechanisms through which helicases affect multiprotein complexes are just beginning to
Thomas Gross et al.
Science (New York, N.Y.), 315(5812), 646-649 (2007-02-03)
In eukaryotes, termination of messenger RNA (mRNA) translation is mediated by the release factors eRF1 and eRF3. Using Saccharomyces cerevisiae as a model organism, we have identified a member of the DEAD-box protein (DBP) family, the DEAD-box RNA helicase and
Christine S Weirich et al.
Molecular cell, 16(5), 749-760 (2004-12-03)
Nuclear export of mRNA in eukaryotic cells is mediated by soluble transport factors and components of the nuclear pore complex (NPC). The cytoplasmically oriented nuclear pore protein Nup159 plays a critical role in mRNA export through its conserved N-terminal domain
C Schmitt et al.
The EMBO journal, 18(15), 4332-4347 (1999-08-03)
Dbp5 is a DEAD-box protein essential for mRNA export from the nucleus in yeast. Here we report the isolation of a cDNA encoding human Dbp5 (hDbp5) which is 46% identical to yDbp5p. Like its yeast homologue, hDbp5 is localized within

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