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D6569

Sigma-Aldrich

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

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Sinonimo/i:

Anti-DDX19B, Anti-DEAD (Asp-Glu-Ala-As) box polypeptide 19B, Anti-DEAD box RNA helicase, Anti-DEAD box protein 19B, Anti-DEAD5

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Coniugato

unconjugated

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

antigen ~53 kDa

Reattività contro le specie

human, mouse, rat

Concentrazione

~1.0 mg/mL

tecniche

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: 0.5-1 μg/mL using HEK-293T cell lysate

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

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

Descrizione generale

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.

Applicazioni

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 0.5-1μg/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.

Azioni biochim/fisiol

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.

Stato fisico

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

Esclusione di responsabilità

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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Prodotti correlati

Codice della classe di stoccaggio

10 - Combustible liquids

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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


Certificati d'analisi (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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