DDX6 Antibody [J2G17] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:100-1:2000 IF1:100

Application
WB, IP, IHC, IF

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
54 kDa 54 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
DDX6 Antibody [J2G17] detects endogenous levels of total DDX6 protein.

Clone
J2G17

Synonym(s)
HLR2, RCK, DDX6, Probable ATP-dependent RNA helicase DDX6, ATP-dependent RNA helicase p54, DEAD box protein 6, Oncogene RCK

Background
DDX6, also known as RCK or p54, is a conserved DEAD‑box RNA helicase that belongs to the DDX6‑like subfamily and functions as a central regulator of cytoplasmic mRNA fate in eukaryotic cells, with prominent localization to processing bodies, stress granules, and discrete nuclear foci in human cell lines. The protein contains the canonical helicase core with conserved motifs for ATP binding, hydrolysis, and RNA interaction, flanked by low‑complexity N‑ and C‑terminal regions that provide docking surfaces for effector proteins and adaptors in distinct mRNP assemblies. The helicase core associates with decapping and 5′–3′ decay factors such as DCP1A, EDC3, EDC4, LSM14A, and XRN1, and this interaction network supports DDX6‑dependent recruitment of translationally repressed mRNAs into P‑bodies and coordination of their decapping and degradation within the deadenylation‑dependent mRNA decay pathway. DDX6 also interacts with translational repressors, including 4E‑T and the CCR4‑NOT complex, thereby coupling cap‑binding protein exchange, translational silencing, and deadenylation, positioning the helicase as a key node that shifts specific transcripts among active polysomes, storage granules, and decay compartments. Association with Argonaute proteins and GW182 family members connects DDX6 to microRNA‑mediated gene silencing, where it supports the assembly of repressed miRNA target mRNPs and their delivery to P‑bodies, integrating small RNA pathways with bulk mRNA turnover. In human cells under normal growth conditions, DDX6 distributes between a diffuse cytosolic pool and distinct P‑bodies defined by colocalization with decapping factors, while under stress it also concentrates in stress granules, forming partially overlapping but functionally distinct mRNP condensates that segregate translationally silenced mRNAs. The protein contains a bipartite nuclear localization signal and a CRM1‑dependent nuclear export sequence, and its nucleocytoplasmic distribution responds to the activity of these signals, thereby permitting shuttling between the nucleus and cytoplasm and providing an additional layer of regulation of the balance between nuclear and cytoplasmic mRNA handling. DDX6 associates with complexes that include PATL1, LSM14A, and other scaffolding factors that determine whether it operates predominantly in translation repression, mRNA storage, or active decay, and distinct partner sets mark mutually exclusive complexes that occupy different cytoplasmic territories and direct different transcript outcomes. In mammalian progenitor and stem cell contexts, DDX6 participates in post‑transcriptional programs that tune the balance between proliferation and differentiation by influencing the stability and translation of mRNAs encoding signaling components and transcriptional regulators, and similar roles extend to regulation of developmental mRNA cohorts across animal systems. Dysregulation of DDX6 expression or complex composition appears in human disease, including cancers where altered helicase levels correlate with changes in the expression of growth‑controlling transcripts, and neurological or developmental settings where perturbation of DDX6‑dependent granule dynamics impacts progenitor function and tissue homeostasis.

Background

DDX6, also known as RCK or p54, is a conserved DEAD‑box RNA helicase that belongs to the DDX6‑like subfamily and functions as a central regulator of cytoplasmic mRNA fate in eukaryotic cells, with prominent localization to processing bodies, stress granules, and discrete nuclear foci in human cell lines. The protein contains the canonical helicase core with conserved motifs for ATP binding, hydrolysis, and RNA interaction, flanked by low‑complexity N‑ and C‑terminal regions that provide docking surfaces for effector proteins and adaptors in distinct mRNP assemblies. The helicase core associates with decapping and 5′–3′ decay factors such as DCP1A, EDC3, EDC4, LSM14A, and XRN1, and this interaction network supports DDX6‑dependent recruitment of translationally repressed mRNAs into P‑bodies and coordination of their decapping and degradation within the deadenylation‑dependent mRNA decay pathway. DDX6 also interacts with translational repressors, including 4E‑T and the CCR4‑NOT complex, thereby coupling cap‑binding protein exchange, translational silencing, and deadenylation, positioning the helicase as a key node that shifts specific transcripts among active polysomes, storage granules, and decay compartments. Association with Argonaute proteins and GW182 family members connects DDX6 to microRNA‑mediated gene silencing, where it supports the assembly of repressed miRNA target mRNPs and their delivery to P‑bodies, integrating small RNA pathways with bulk mRNA turnover. In human cells under normal growth conditions, DDX6 distributes between a diffuse cytosolic pool and distinct P‑bodies defined by colocalization with decapping factors, while under stress it also concentrates in stress granules, forming partially overlapping but functionally distinct mRNP condensates that segregate translationally silenced mRNAs. The protein contains a bipartite nuclear localization signal and a CRM1‑dependent nuclear export sequence, and its nucleocytoplasmic distribution responds to the activity of these signals, thereby permitting shuttling between the nucleus and cytoplasm and providing an additional layer of regulation of the balance between nuclear and cytoplasmic mRNA handling. DDX6 associates with complexes that include PATL1, LSM14A, and other scaffolding factors that determine whether it operates predominantly in translation repression, mRNA storage, or active decay, and distinct partner sets mark mutually exclusive complexes that occupy different cytoplasmic territories and direct different transcript outcomes. In mammalian progenitor and stem cell contexts, DDX6 participates in post‑transcriptional programs that tune the balance between proliferation and differentiation by influencing the stability and translation of mRNAs encoding signaling components and transcriptional regulators, and similar roles extend to regulation of developmental mRNA cohorts across animal systems. Dysregulation of DDX6 expression or complex composition appears in human disease, including cancers where altered helicase levels correlate with changes in the expression of growth‑controlling transcripts, and neurological or developmental settings where perturbation of DDX6‑dependent granule dynamics impacts progenitor function and tissue homeostasis.

References
https://pubmed.ncbi.nlm.nih.gov/32283676/ https://pubmed.ncbi.nlm.nih.gov/28216671/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%