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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

Synonym(s):

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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~53 kDa

species reactivity

human, mouse, rat

concentration

~1.0 mg/mL

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

UniProt accession no.

Q9UMR2

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

application

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.

Biochem/physiol Actions

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.

Physical form

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

ppe

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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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