Recombinant Human DDX11 protein is a Human Full Length protein, in the 1 to 970 aa range, expressed in Wheat germ and suitable for ELISA, WB.
M A N E T Q K V G A I H F P F P F T P Y S I Q E D F M A E L Y R V L E A G K I G I F E S P T G T G K S L S L I C G A L S W L R D F E Q K K R E E E A R L L E T G T G P L H D E K D E S L C L S S S C E G A A G T P R P A G E P A W V T Q F V Q K K E E R D L V D R L K A E Q A R R K Q R E E R L Q Q L Q H R V Q L K Y A A K R L R Q E E E E R E N L L R L S R E M L E T G P E A E R L E Q L E S G E E E L V L A E Y E S D E E K K V A S R V D E D E D D L E E E H I T K I Y Y C S R T H S Q L A Q F V H E V K K S P F G K D V R L V S L G S R Q N L C V N E D V K S L G S V Q L I N D R C V D M Q R S R H E K K K G A E E E K P K R R R Q E K Q A A C P F Y N H E Q M G L L R D E A L A E V K D M E Q L L A L G K E A R A C P Y Y G S R L A I P A A Q L V V L P Y Q M L L H A A T R Q A A G I R L Q D Q V V I I D E A H N L I D T I T G M H S V E V S G S Q L C Q A H S Q L L Q Y V E R Y G K R L K A K N L M Y L K Q I L Y L L E K F V A V L G G N I K Q N P N T Q S L S Q T G T E L K T I N D F L F Q S Q I D N I N L F K V Q R Y C E K S M I S R K L F G F T E R Y G A V F S S R E Q P K L A G F Q Q F L Q S L Q P R T T E A L A A P A D E S Q A S T L R P A S P L M H I Q G F L A A L T T A N Q D G R V I L S R Q G S L S Q S T L K F L L L N P A V H F A Q V V K E C R A V V I A G G T M Q P V S D F R Q Q L L A C A G V E A E R V V E F S C G H V I P P D N I L P L V I C S G I S N Q P L E F T F Q K R E L P Q M M D E V G R I L C N L C G V V P G G V V C F F P S Y E Y L R Q V H A H W E K G G L L G R L A A R K K I F Q E P K S A H Q V E Q V L L A Y S R C I Q A C G Q E R G Q V T G A L L L S V V G G K M S E G I N F S D N L G R C V V M V G M P F P N I R S A E L Q E K M A Y L D Q T L S P R P G T P R E G S G G E P V H E G R Q P V H R Q G H Q A P E G F C Q R S A P G P A I C P A P C P G Q A A G L D P S P C G G Q S Y L W P R H C C C A E V S P G E V G L F L M G N H A T A W R R A L P L S C P L E T V F V V G V V C G D P V T K V K P R R R V W S P E C C Q D P G T G V S S R R R K W G N P E
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Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application WB | Reactivity Reacts | Dilution info - | Notes - |
DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis (PubMed:10648783, PubMed:21854770, PubMed:23797032, PubMed:26089203, PubMed:26503245). Its double-stranded DNA helicase activity requires either a minimal 5'-single-stranded tail length of approximately 15 nt (flap substrates) or 10 nt length single-stranded gapped DNA substrates of a partial duplex DNA structure for helicase loading and translocation along DNA in a 5' to 3' direction (PubMed:10648783, PubMed:18499658, PubMed:22102414). The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended up to 500 bp by the replication protein A (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC) complex activities (PubMed:18499658). Shows also ATPase- and helicase activities on substrates that mimic key DNA intermediates of replication, repair and homologous recombination reactions, including forked duplex, anti-parallel G-quadruplex and three-stranded D-loop DNA molecules (PubMed:22102414, PubMed:26503245). Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage (PubMed:23797032). Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity (PubMed:26503245). Cooperates also with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation (PubMed:17105772, PubMed:18499658, PubMed:20124417, PubMed:23116066, PubMed:23797032). Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner; and hence it may contribute in Okazaki fragment processing at DNA replication fork during lagging strand DNA synthesis (PubMed:18499658). Its ability to function at DNA replication fork is modulated by its binding to long non-coding RNA (lncRNA) cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase activity and binding to DNA replicating regions (PubMed:27477908). Also plays a role in heterochromatin organization (PubMed:21854770). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery (PubMed:26089203). Plays a role in embryonic development and prevention of aneuploidy (By similarity). Involved in melanoma cell proliferation and survival (PubMed:23116066). Associates with chromatin at DNA replication fork regions (PubMed:27477908). Binds to single- and double-stranded DNAs (PubMed:18499658, PubMed:22102414, PubMed:9013641). (Microbial infection) Required for bovine papillomavirus type 1 regulatory protein E2 loading onto mitotic chromosomes during DNA replication for the viral genome to be maintained and segregated.
CHL1, CHLR1, KRG2, DDX11, ATP-dependent DNA helicase DDX11, CHL1-related protein 1, DEAD/H-box protein 11, DNA 5'-3' helicase DDX11, Keratinocyte growth factor-regulated gene 2 protein, hCHLR1, KRG-2
Recombinant Human DDX11 protein is a Human Full Length protein, in the 1 to 970 aa range, expressed in Wheat germ and suitable for ELISA, WB.
pH: 8
Constituents: 0.79% Tris HCl, 0.31% Glutathione
DNA-dependent ATPase and ATP-dependent DNA helicase that participates in various functions in genomic stability, including DNA replication, DNA repair and heterochromatin organization as well as in ribosomal RNA synthesis (PubMed:10648783, PubMed:21854770, PubMed:23797032, PubMed:26089203, PubMed:26503245). Its double-stranded DNA helicase activity requires either a minimal 5'-single-stranded tail length of approximately 15 nt (flap substrates) or 10 nt length single-stranded gapped DNA substrates of a partial duplex DNA structure for helicase loading and translocation along DNA in a 5' to 3' direction (PubMed:10648783, PubMed:18499658, PubMed:22102414). The helicase activity is capable of displacing duplex regions up to 100 bp, which can be extended up to 500 bp by the replication protein A (RPA) or the cohesion CTF18-replication factor C (Ctf18-RFC) complex activities (PubMed:18499658). Shows also ATPase- and helicase activities on substrates that mimic key DNA intermediates of replication, repair and homologous recombination reactions, including forked duplex, anti-parallel G-quadruplex and three-stranded D-loop DNA molecules (PubMed:22102414, PubMed:26503245). Plays a role in DNA double-strand break (DSB) repair at the DNA replication fork during DNA replication recovery from DNA damage (PubMed:23797032). Recruited with TIMELESS factor upon DNA-replication stress response at DNA replication fork to preserve replication fork progression, and hence ensure DNA replication fidelity (PubMed:26503245). Cooperates also with TIMELESS factor during DNA replication to regulate proper sister chromatid cohesion and mitotic chromosome segregation (PubMed:17105772, PubMed:18499658, PubMed:20124417, PubMed:23116066, PubMed:23797032). Stimulates 5'-single-stranded DNA flap endonuclease activity of FEN1 in an ATP- and helicase-independent manner; and hence it may contribute in Okazaki fragment processing at DNA replication fork during lagging strand DNA synthesis (PubMed:18499658). Its ability to function at DNA replication fork is modulated by its binding to long non-coding RNA (lncRNA) cohesion regulator non-coding RNA DDX11-AS1/CONCR, which is able to increase both DDX11 ATPase activity and binding to DNA replicating regions (PubMed:27477908). Also plays a role in heterochromatin organization (PubMed:21854770). Involved in rRNA transcription activation through binding to active hypomethylated rDNA gene loci by recruiting UBTF and the RNA polymerase Pol I transcriptional machinery (PubMed:26089203). Plays a role in embryonic development and prevention of aneuploidy (By similarity). Involved in melanoma cell proliferation and survival (PubMed:23116066). Associates with chromatin at DNA replication fork regions (PubMed:27477908). Binds to single- and double-stranded DNAs (PubMed:18499658, PubMed:22102414, PubMed:9013641).
Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.
DDX11 also known as ChlR1 is a DNA helicase enzyme that belongs to the DEAD/H box family characterized by their Asp-Glu-Ala-Asp (DEAD) motifs. With a molecular mass of approximately 100 kDa DDX11 plays a role in unwinding DNA duplexes which is essential for DNA replication and repair processes. This protein is expressed in various tissues with higher expression levels observed in proliferating cells due to their increased demand for DNA replication machinery. The helicase activity of DDX11 facilitates the resolution of complex DNA structures supporting genomic stability.
This helicase functions within the cellular nucleus where it assists in chromosome cohesion and accurate chromosome segregation during cell division. As part of the cohesin complex DDX11 contributes to the stabilization of sister chromatid cohesion maintaining proper chromosome alignment. The cohesin complex encompasses several proteins including SMC1 and SMC3 which work collaboratively to ensure correct mitotic and meiotic division. By participating in this complex DDX11 plays an important role in preserving genomic integrity during cellular division and avoiding aneuploidy.
DDX11 is integral to the DNA damage response and DNA replication stress pathways. In these contexts it interacts with proteins like ATR (Ataxia Telangiectasia and Rad3 related protein) and Fanconi anemia group proteins coordinating cellular responses to DNA damage and replication impediments. The interaction with ATR emphasizes DDX11's involvement in the ATR-dependent checkpoint signaling pathway enabling cells to delay cell cycle progression in response to genotoxic stress. This coordination helps prevent errors during DNA replication and preserves genome fidelity.
DDX11 mutations and dysregulation have been associated with Warsaw Breakage Syndrome characterized by growth retardation and developmental abnormalities. In this condition the helicase's impaired function leads to defects in sister chromatid cohesion often observed as chromosomal breakage and rearrangements. Moreover abnormalities in DDX11 function can correlate with cancer development as faulty DNA repair and chromosomal instability are common features of tumorigenesis. In such scenarios connections with proteins such as BRCA1 may emerge given BRCA1's role in maintaining genomic stability and DDX11's contribution to DNA repair mechanisms.
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ab158272 on a 12.5% SDS-PAGE stained with Coomassie Blue.
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