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SAB2500304

Sigma-Aldrich

Anti-DDX5/P68 RNA helicase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Sinônimo(s):

Anti-DEAD/H box polypeptide 5, Anti-G17P1, Anti-HLR1, Anti-HUMP68

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

goat

Nível de qualidade

100

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

reatividade de espécies

mouse, human, rat

técnica(s)

immunohistochemistry: suitable
indirect ELISA: suitable
indirect immunofluorescence: suitable
western blot: suitable

nº de adesão UniProt

P17844

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... DDX5(1655)

Descrição geral

DDX5 (DEAD, Asp-Glu-Ala-Asp, box helicase 5) is a multifunctional protein belonging to the DEAD box family of RNA helicases. It consists of twelve conserved motifs (including the signature D-E-A-D motif) forming a conserved ′helicase′ central domain, which plays an important role in the RNA metabolism.
DEAD-box helicase 5 (DDX5) is encoded by the gene mapped to human chromosome 17q23.3–q24.2.

Imunogênio

Peptide with sequence C-PMIGYPMPTGYSQ from the C Terminus of the protein sequence according to NP_004387.1.

Aplicação

Anti-DDX5/P68 RNA helicase antibody produced in goat is suitable for indirect immunofluorescence, indirect ELISA, and western blot applications.

Ações bioquímicas/fisiológicas

DDX5 (DEAD, Asp-Glu-Ala-Asp, box helicase 5) is associated with the regulation of pre-mRNA splicing mechanism. It acts as a transcriptional coactivator to control alternative splicing during the formation of spliceosome. DDX5 provides stability to the RNA secondary structure during several activities such as in the translation initiation, nuclear and mitochondrial splicing. It facilitates the unwinding as well as detachment of protein part from RNA. The protein also participates in the estrogen- and androgen-signaling pathway.

Características e benefícios

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

forma física

Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.

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Nº do produto
Descrição
Preços

Pictogramas

Exclamation mark
GHS07

Palavra indicadora

Warning

Frases de perigo

H315,H319

Declarações de precaução

P305 + P351 + P338

Classificações de perigo

Eye Irrit. 2 - Skin Irrit. 2

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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High-resolution analysis of chromosomal imbalances using the Affymetrix 10K SNP genotyping chip.
Alexander H, et al
Genomics, 85(3), 392-400 (2005)
Samaan Samaan et al.
Nucleic acids research, 42(4), 2197-2207 (2013-11-28)
Estrogen and androgen receptors (ER and AR) play key roles in breast and prostate cancers, respectively, where they regulate the transcription of large arrays of genes. The activities of ER and AR are controlled by large networks of protein kinases
Frances V Fuller-Pace
Biochimica et biophysica acta, 1829(8), 756-763 (2013-03-26)
Members of the DEAD box family of RNA helicases, which are characterised by the presence of twelve conserved motifs (including the signature D-E-A-D motif) within a structurally conserved 'helicase' core, are involved in all aspects of RNA metabolism. Apart from
Ulrike Rappe et al.
The Journal of biological chemistry, 289(18), 12421-12434 (2014-03-20)
The armadillo repeat protein ARVCF is a component of adherens junctions. Similar to related proteins, such as p120-catenin and β-catenin, with known signaling functions, localization studies indicate a cytoplasmic and a nuclear pool of ARVCF. We find that ARVCF interacts

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