Human DDX5 blocking peptide

Name: Human DDX5 blocking peptide
SKU: CDBP0986
Rating: 5 (1 reviews)

Synthetic Human DDX5 blocking peptide for Apuri, BL, ELISA

COA

SDS

Datasheet

Summary

Product Overview

Blocking/Immunizing peptide for anti-DDX5/p68 RNA helicase antibody

Target

DDX5 / p68 RNA helicase

Nature

Synthetic

Tag/Conjugate

Unconjugated

Application Notes

For in vitro research use only. Not intended for any diagnostic or therapeutic purpose. Not for human or animal consumption.

Format

Lyophilized powder

Preservative

None

Storage

Shipped at ambient temperature, store at -20°C.

Entrez Gene ID

1655

Antigen Description

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which is a RNA-dependent ATPase, and also a proliferation-associated nuclear antigen, specifically reacting with the simian virus 40 tumor antigen. This gene consists of 13 exons, and alternatively spliced transcripts containing several intron sequences have been detected, but no isoforms encoded by these transcripts have been identified.

Function

ATP binding; ATP-dependent helicase activity; RNA helicase activity; RNA helicase activity; androgen receptor binding; estrogen receptor binding; hydrolase activity; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; nucle

Synonyms

DDX5; DEAD (Asp-Glu-Ala-Asp) box helicase 5; DEAD (Asp Glu Ala Asp) box polypeptide 5 , DEAD/H (Asp Glu Ala Asp/His) box polypeptide 5 (RNA helicase, 68kD) , G17P1, HLR1; probable ATP-dependent RNA helicase DDX5; p68; DEAD box-5; RNA helicase p68; DEAD box protein 5; ATP-dependent RNA helicase DDX5; DEAD (Asp-Glu-Ala-Asp) box polypeptide 5; DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 5 (RNA helicase, 68kD); HLR1; G17P1; HUMP68; DKFZp434E109; DKFZp686J01190;

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

The tandem Agenet domain of fragile X mental retardation protein interacts with FUS

SCIENTIFIC REPORTS

Authors: He, Qingzhong; Ge, Wei

Abstract

The tandem Agenet domain (TAD) of fragile X mental retardation protein (FMRP) protein is considered to be a member of the methyl-lysine-binding Tudor domain "Royal family". Several groups have reported that the TAD binds with methylated histones and plays a role in DNA damage responses. FMRP is a RNA-binding protein predominantly resident in cytoplasm. Therefore, in this study, we identified DDX5, FUS, EWSR1 and LSM14A as TAD-interacting proteins sensitive to F32L and/or Y96L mutation by pull-down assays and mass spectrometry. We also showed that the interaction is potentially mediated by RGG/RG motifs. Furthermore, when FMRP was knocked-down, translocation of exogenously expressed wild-type FUS and disease-related mutant R514G was observed. This study may provide a novel insight into FMRP involvement in the intracellular localization of FUS and pathology of FUS-related amyotrophic lateral sclerosis.

PRD-1, a Component of the Circadian System of Neurospora crassa, Is a Member of the DEAD-box RNA Helicase Family

JOURNAL OF BIOLOGICAL RHYTHMS

Authors: Adhvaryu, Keyur; Firoozi, Ghazaleh; Motavaze, Kamyar; Lakin-Thomas, Patricia

Abstract

The circadian rhythms found in almost all organisms are driven by molecular oscillators, including transcription/translation feedback loops (TTFLs). However, TTFL-independent oscillators can drive rhythms in both eukaryotes and prokaryotes. The fungus Neurospora crassa is a model organism for studying the molecular mechanism of the circadian clock. Although a circadian TTFL involving the proteins FRQ, WC-1, and WC-2 is well-characterized in N. crassa, rhythms can still be observed in the absence of this feedback loop. These rhythms are said to be driven by 1 or more FRQ-less oscillator(s) (FLOs). The prd-1 mutation lengthens the period in frq wild type and was previously shown to severely disrupt FRQ-less rhythms in frq null mutants under several different conditions; therefore, the prd-1 gene product is a candidate for a component of a FLO. We report here that prd-1 also disrupts free-running rhythms in wc-1 null mutants, confirming its effects on FRQ-less rhythms. We have now mapped and identified the prd-1 gene as NCU07839, a DEAD-box RNA helicase dbp-2. Complementation with the wild-type gene corrects the rhythm defects of the prd-1 mutant in the complete circadian system (when the FRQ-based TTFL is intact) and also the free-running FRQ-less rhythm on low choline. A PRD-1-GFP fusion protein localizes to the nucleus. The prd-1 mutant has a single base pair change in the first base of an intron that results in abnormally spliced transcripts. FRQ-less rhythms on low choline, or entrained to heat pulses, were only marginally affected in strains carrying deletions of 2 other RNA helicases (prd-6 and msp-8). We conclude that PRD-1 is a member of an RNA helicase family that may be specifically involved in regulating rhythmicity in N. crassa in both the complete circadian system and FLO(s).