Recombinant Human Atp-Dependent Dna/Rna Helicase Dhx36 (DHX36) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00547P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Atp-Dependent Dna/Rna Helicase Dhx36 (DHX36) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-00547P
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Product Overview

Description Recombinant Human Atp-Dependent Dna/Rna Helicase Dhx36 (DHX36) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q9H2U1
Target Symbol DHX36
Synonyms (DEAD/H box polypeptide 36)(DEAH-box protein 36)(G4-resolvase-1)(G4R1)(MLE-like protein 1)(RNA helicase associated with AU-rich element protein)
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence ERREEQIVQLLNSVQAKNDKESEAQISWFAPEDHGYGTEVSTKNTPCSENKLDIQEKKLINQEKKMFRIRNRSYIDRDSEYLLQENEPDGT
Expression Range 89-179aa
Protein Length Partial
Mol. Weight 18.2 kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Multifunctional ATP-dependent helicase that unwinds G-quadruplex (G4) structures. Plays a role in many biological processes such as genomic integrity, gene expression regulations and as a sensor to initiate antiviral responses. G4 structures correspond to helical structures containing guanine tetrads. Binds with high affinity to and unwinds G4 structures that are formed in nucleic acids (G4-ADN and G4-RNA). Plays a role in genomic integrity. Converts the G4-RNA structure present in telomerase RNA template component (TREC) into a double-stranded RNA to promote P1 helix formation that acts as a template boundary ensuring accurate reverse transcription. Plays a role in transcriptional regulation. Resolves G4-DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL and positively regulates their expression. Plays a role in post-transcriptional regulation. Unwinds a G4-RNA structure located in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced DNA damage. Binds to the precursor-microRNA-134 (pre-miR-134) terminal loop and regulates its transport into the synapto-dendritic compartment. Involved in the pre-miR-134-dependent inhibition of target gene expression and the control of dendritic spine size. Plays a role in the regulation of cytoplasmic mRNA translation and mRNA stability. Binds to both G4-RNA structures and alternative non-quadruplex-forming sequence within the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein expression. Binds to both G4-RNA structure in the 5'-UTR and AU-rich elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either stimulate protein translation or induce mRNA decay in an ELAVL1-dependent manner, respectively. Binds also to ARE sequences present in several mRNAs mediating exosome-mediated 3'-5' mRNA degradation. Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA decay. Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of proinflammatory cytokines via the adapter molecule TICAM1. Required for early embryonic development and hematopoiesis. Involved in the regulation of cardioblast differentiation and proliferation during heart development. Involved in spermatogonia differentiation. May play a role in ossification.
Subcellular Location Nucleus. Cytoplasm. Cytoplasm, cytosol. Cytoplasm, Stress granule. Nucleus speckle. Chromosome, telomere. Mitochondrion. Perikaryon. Cell projection, dendrite. Cell projection, axon.; [Isoform 1]: Nucleus. Cytoplasm.; [Isoform 2]: Nucleus. Cytoplasm.
Protein Families DEAD box helicase family, DEAH subfamily
Database References

HGNC: 14410

OMIM: 612767

KEGG: hsa:170506

STRING: 9606.ENSP00000417078

UniGene: PMID: 27407146

  • RHAU mediates the unfolding of DNA and RNA quadruplexes. PMID: 28065761
  • The study provides the first evidence that the unfolding kinetics of a G-quadruplex can be modulated by different nucleotide-bound states of the RHAU helicase. PMID: 28069994
  • RHAU binds to an adenosine-rich region near the 3'-end of the long non-coding RNA BC200. PMID: 26740632
  • present a model showing that a replication fork disrupting a T-loop could create a 5' quadruplex with an opened 3'tail structure that is recognized by G4R1 PMID: 26172836
  • we identify a novel function of DHX36 to facilitate viral RNA recognition PMID: 24651521
  • Used an integrated approach that includes small angle x-ray scattering, nuclear magnetic resonance spectroscopy, circular dichroism, and dynamic light scattering methods to demonstrate the recognition of G-quadruplexes by the N-terminal domain of RHAU. PMID: 24151078
  • Data supports a helicase function of RHAU on an intramolecular RNA quadruplex and show that the enzyme is capable of completely converting quadruplex RNA to a stable duplex. PMID: 22238380
  • Data show that hnRNPA1/A2, HuR and DAZAP1 splicing factors and DHX36 RNA helicase bind to the ISE, with hnRNPA1 acting negatively and DAZAP1 positively on splicing selection PMID: 21858080
  • The helicase domain of DHX36 does not mediate telomerase RNA (hTR) binding; instead, hTR interacts with the N-terminal accessory domain of DHX36 known to bind specifically to the parallel-strand G-quadruplex substrates resolved by the helicase domain. PMID: 21149580
  • The amino-terminal region of RHAU is essential for RHAU to bind G4 structures and within this region the evolutionary conserved RSM (RHAU-specific motif) domain is a major affinity and specificity determinant PMID: 20472641
  • DHX9/DHX36 represent the MyD88-dependent DNA sensors in the cytosol of plasmacytoid dendritic cells and suggest a much broader role for DHX helicases in viral sensing PMID: 20696886
  • DHX36 protein is responsible for the majority of tetramolecular G4-DNA resolvase activity PMID: 16150737
  • RHAU has a dual function, being involved in both the synthesis and degradation of mRNA in different subcellular compartments. PMID: 18279852
  • the RNA quadruplex resolving enzymatic activity associated with G4R1/RHAU and its exceptional binding affinity, suggesting a potential novel role for G4R1/RHAU in targeting in vivo RNA quadruplex structures PMID: 18842585
  • RHAU is the fourth RNA helicase detected in SGs, after rck/p54, DDX3, and eIF4A, and its association with SGs is dynamic and mediated by an RHAU-specific RNA-binding domain PMID: 18854321
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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