DHX9 Antibody [E8M24] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Lane 1: MCF7, Lane 2: Hela, Lane 3: HepG2, Lane 4: Jurkat

Usage Information

Dilution
WB1:5000-1:50000 IHC1:1000-1:4000 IF1:50-1:500

Application
WB, IP, IHC, IF, ELISA

Reactivity
Human, Mouse, Rat

Source
Mouse 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
141 kDa 140 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Mouse brain tissue; MCF7 cells; HeLa cells; HEK-293 cells; HepG2 cells; Jurkat cells; K-562 cells; THP-1 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
DHX9 Antibody [E8M24] detects endogenous levels of total DHX9 protein.

Clone
E8M24

Synonym(s)
DHX9; ATP-dependent RNA helicase A; EC:3.6.4.13; DEAH box protein 9; DExH-box helicase 9; Leukophysin (LKP); Nuclear DNA helicase II (NDH II); RNA helicase A; DDX9; LKP; NDH2

Background
DHX9 (DExH-box helicase 9, also known as RNA helicase A or nuclear DNA helicase II) is a 1,200-amino-acid SF2 family helicase that is ubiquitously expressed and essential for embryonic development, functioning to unwind DNA and RNA structures in the 3'-5' direction using all NTPs and dNTPs as energy sources. Its core consists of RecA-like helicase domains (motifs I–VI, residues ~380–830) that form an NTP-binding cleft with a flexible hinge, flanked by N-terminal double-stranded RNA-binding domains (dsRBD1/2) for substrate recognition, a minimal transactivation domain (MTAD) for RNA polymerase II association, and C-terminal helicase-associated (HA2), OB-fold, and RGG-box motifs that specifically recognize G-quadruplexes and R-loops. The dsRBD2 domain stabilizes the RNA channel, while the OB-fold and RGG-box grip single-stranded nucleic acid tails; the protein undergoes conformational shifts between an inactive, closed state (with disordered dsRBD2) and an active, open, RNA-anchored state triggered by NTP and RNA binding. DHX9 resolves R-loops by recruiting TDRD3 to prevent replication stress and double-strand breaks, unwinds G-quadruplexes and inverted repeats (IRAlus) to suppress circRNA biogenesis, facilitates BRCA1 recruitment for homologous recombination repair, promotes pre-mRNA splicing through interactions with U2AF65 and SRSF1, and coactivates c-Myc and STAT6 transcription. NTP hydrolysis drives 3'-tail anchored translocation and remodeling of RNA:DNA hybrids and multi-stranded complexes, with the dsRBD2/RecA2 β-hairpin gripping RNA backbones and OB/HA2 rotation opening channels for complex nucleic acid substrates. Dysregulation of DHX9 is implicated in cancer (upregulated in HCC and breast cancer, promoting angiogenesis and invasion via VEGF and c-Myc), viral replication (through enhancer binding in HIV and JCV), and neurodegeneration (due to unresolved G-quadruplex toxicity).

Background

DHX9 (DExH-box helicase 9, also known as RNA helicase A or nuclear DNA helicase II) is a 1,200-amino-acid SF2 family helicase that is ubiquitously expressed and essential for embryonic development, functioning to unwind DNA and RNA structures in the 3'-5' direction using all NTPs and dNTPs as energy sources. Its core consists of RecA-like helicase domains (motifs I–VI, residues ~380–830) that form an NTP-binding cleft with a flexible hinge, flanked by N-terminal double-stranded RNA-binding domains (dsRBD1/2) for substrate recognition, a minimal transactivation domain (MTAD) for RNA polymerase II association, and C-terminal helicase-associated (HA2), OB-fold, and RGG-box motifs that specifically recognize G-quadruplexes and R-loops. The dsRBD2 domain stabilizes the RNA channel, while the OB-fold and RGG-box grip single-stranded nucleic acid tails; the protein undergoes conformational shifts between an inactive, closed state (with disordered dsRBD2) and an active, open, RNA-anchored state triggered by NTP and RNA binding. DHX9 resolves R-loops by recruiting TDRD3 to prevent replication stress and double-strand breaks, unwinds G-quadruplexes and inverted repeats (IRAlus) to suppress circRNA biogenesis, facilitates BRCA1 recruitment for homologous recombination repair, promotes pre-mRNA splicing through interactions with U2AF65 and SRSF1, and coactivates c-Myc and STAT6 transcription. NTP hydrolysis drives 3'-tail anchored translocation and remodeling of RNA:DNA hybrids and multi-stranded complexes, with the dsRBD2/RecA2 β-hairpin gripping RNA backbones and OB/HA2 rotation opening channels for complex nucleic acid substrates. Dysregulation of DHX9 is implicated in cancer (upregulated in HCC and breast cancer, promoting angiogenesis and invasion via VEGF and c-Myc), viral replication (through enhancer binding in HIV and JCV), and neurodegeneration (due to unresolved G-quadruplex toxicity).

References
https://pubmed.ncbi.nlm.nih.gov/37860960/ https://pubmed.ncbi.nlm.nih.gov/27034008/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

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%