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SAB2500304

Sigma-Aldrich

Anti-DDX5/P68 RNA helicase antibody produced in goat

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

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

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

goat

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

mouse, human, rat

Technique(s)

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... DDX5(1655)

Description générale

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.

Immunogène

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

Application

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

Actions biochimiques/physiologiques

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.

Caractéristiques et avantages

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.

Forme physique

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

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Pictogrammes

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Mention d'avertissement

Warning

Mentions de danger

Conseils de prudence

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
High-resolution analysis of chromosomal imbalances using the Affymetrix 10K SNP genotyping chip.
Alexander H, et al
Genomics, 85(3), 392-400 (2005)
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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