Recombinant Human Probable Atp-Dependent Rna Helicase Ddx5 (DDX5) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-02881P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) DDX5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) DDX5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) DDX5.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) DDX5.

Recombinant Human Probable Atp-Dependent Rna Helicase Ddx5 (DDX5) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-02881P
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Product Overview

Description Recombinant Human Probable Atp-Dependent Rna Helicase Ddx5 (DDX5) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P17844
Target Symbol DDX5
Synonyms ATP dependent RNA helicase DDX5; DDX 5; Ddx5; DDX5_HUMAN; DEAD (Asp Glu Ala Asp) box helicase 5; DEAD (Asp Glu Ala Asp) box polypeptide 5; DEAD box 5; DEAD box protein 5; DEAD/H (Asp Glu Ala Asp/His) box polypeptide 5 (RNA helicase; 68kD); G17P1; HELR; HLR1; HUMP68; P68; p68 RNA helicase; Probable ATP dependent RNA helicase DDX5; Probable ATP-dependent RNA helicase DDX5; RNA helicase p68
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVEICIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQTSFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ
Expression Range 1-614aa
Protein Length Full Length
Mol. Weight 74.1 kDa
Research Area Epigenetics And Nuclear Signaling
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 Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms.
Subcellular Location Nucleus. Nucleus, nucleolus. Cytoplasm.
Protein Families DEAD box helicase family, DDX5/DBP2 subfamily
Database References

Gene Functions References

  1. RIP-seq analysis in HEK293T cells identifies a complete repertoire of DDX5/p68 interacting transcripts including LOC284454 lncRNA. PMID: 29227193
  2. Results showed that DDX5 was significantly up-regulated in gastric cancer tissues and revealed a novel role of DDX5 in gastric cancer cell proliferation via the mTOR pathway. PMID: 28216662
  3. DDX5 is shown to be involved in RNA metabolism and viral infection, especially for RNA virus which seems to hijack host DDX5 to facilitate its own replication. However, DDX5 exhibits a role in antiviral responses during HBV and MYXV infection. Its opposite roles between DNA and RNA infection likely reflect the different modes of the biosynthesis of RNA and DNA viruses. [review] PMID: 29642538
  4. A significant overlap between hnRNPA1 and DDX5 splicing targets and they share many closely linked binding sites. PMID: 30042133
  5. The role of DDX5 in regulating esophageal cancer cell proliferation and tumorigenesis.DDX5 is highly expressed in esophageal cancer. PMID: 28244855
  6. Downregulation of p68 RNA Helicase (DDX5) Activates a Survival Pathway Involving mTOR and MDM2 Signals.( PMID: 28557706
  7. Results show refined biochemical and biological comparison of yeast Dbp2 and human DDX5 enzymes. Human DDX5 possesses a 10-fold higher unwinding activity than Dbp2, partially due to the presence of a mammalian/avian specific C-terminal extension. Also, ectopic expression of DDX5 rescues the cold sensitivity, cryptic initiation defects, and impaired glucose import in dbp2Delta cells, suggesting functional conservation. PMID: 28411202
  8. p53 gain-of-function mutations accelerate endometrial carcinoma progression and metastasis by interfering with Drosha and p68 binding and pri-miR-26a-1 processing, resulting in reduced miR-26a expression and EZH2 overexpression. PMID: 26587974
  9. Cervical cancer cell DDX5 gene is transcriptionally upregulated by calcitriol through a VDRE located in its proximal promoter. PMID: 26314252
  10. Systematic Determination of Human Cyclin Dependent Kinase (CDK)-9 Interactome Identifies Novel Functions in RNA Splicing Mediated by the DEAD Box DDX5 and DDX17 RNA Helicases PMID: 26209609
  11. LMTK3 escapes tumour suppressor miRNAs via sequestration of DDX5. PMID: 26739063
  12. The data provide a model in which p68 and p53 interplay regulates PLK1 expression, and which describes the behavior of these molecules, and the outcome of their interaction, in human breast cancer. PMID: 24626184
  13. Results show that a new mechanism of oncogenesis is attributed to p68 by upregulation of AKT and consequent nuclear exclusion and degradation of tumor suppressor FOXO3a. PMID: 25745998
  14. DDX5 played an important role in the proliferation and tumorigenesis of non-small-cell lung cancer cells by activating the beta-catenin signaling pathway. PMID: 26212035
  15. study shows that correction of p68 may reduce toxicity of the mutant RNAs in DM1 and in DM2 PMID: 26080402
  16. Data indicate that cyclooxygenase 2 (COX-2) correlates inversely to microRNA 183 (miR-183) and directly to DEAD-box helicase p68 (DDX5). PMID: 25963660
  17. DDX5 protein is essential for normal cell proliferation; (2) the transition from G1 to S/G2 phase is accompanied by an increase of DDX5 protein concentration in the cells. PMID: 26035968
  18. AML is dependent on DDX5 and that inhibiting DDX5 expression slows AML cell proliferation. PMID: 24910429
  19. Downregulation of DDX5 and DDX17 protein expression during myogenesis and epithelial-to-mesenchymal transdifferentiation contributes to the switching of splicing programs during these processes. PMID: 24910439
  20. Data indicate that armadillo repeat protein ARVCF interacts with the splicing factors the splicing factor SRSF1 (SF2/ASF), the RNA helicase p68 (DDX5), and the heterogeneous nuclear ribonucleoprotein hnRNP H2. PMID: 24644279
  21. In conclusion, authors identified DDX5 as a positive regulator for Japanese encephalitis virus replication via its binding to viral 3' UTR. PMID: 24035833
  22. DDX5 facilitates HIV-1 replication as a cellular co-factor of Rev. PMID: 23741449
  23. DDX5 might be critical for NOTCH1-mediated T-ALL pathogenesis and thus is a potential new target for modulating the Notch signaling in leukemia PMID: 23108395
  24. p68, in the presence of Ca-calmodulin, can function as a microtubule motor. PMID: 23322042
  25. Results show a novel role for DDX5 in cancer cell proliferation and suggest DDX5 as a therapeutic target in breast cancer treatment. PMID: 22750847
  26. High p68 RNA helicase expression is associated with glioma. PMID: 22810421
  27. Data indicate that transcriptional coregulator ddx5/ddx17 RNA helicases can simultaneously regulate the transcriptional activity and alternative splicing of NFAT5 transcription factor. PMID: 22266867
  28. RNA helicases Ddx17 and Ddx5 contribute to tumor-cell invasiveness by regulating alternative splicing of several DNA- and chromatin-binding factors, including the macroH2A1 histone. PMID: 23022728
  29. The DEAD box RNA helicase p68, also referred to as DDX5, directly interacts with VDR. PMID: 22476084
  30. there is a direct interaction between DDX5 and NS5B and DDX5 has two independent NS5B-binding sites PMID: 22640416
  31. High DDX5 is associated with basal breast cancer cells. PMID: 22086602
  32. Using an RNA affinity pulldown-coupled mass spectrometry approach the study identified DDX5/RNA helicase p68 as an activator of TAU exon 10 splicing. PMID: 21343338
  33. a striking inverse association of p68 and delta133p53 expression in primary breast cancers was identified. PMID: 20818423
  34. DEAD-box RNA helicase p68 (DDX5) and its associated noncoding RNA, steroid receptor RNA activator (SRA), form a complex with CTCF that is essential for insulator function PMID: 20966046
  35. Pleiotropic effects of p300-mediated acetylation on p68 and p72 RNA helicase. PMID: 20663877
  36. crystallization and preliminary diffraction analysis of N-terminal region of DDX5 is reported.X-ray diffraction data were processed to a resolution of 2.7 A. PMID: 20124720
  37. DDX5 is a repressor of fibrogenic genes in HSCs through interaction with transcriptional complexes. PMID: 20022962
  38. Essential for pre-mrna splicing in vitro; may function in destabilizing the U1-5'ss interaction. Depletion of p68 RNA helicase arrested spliceosome assembly at the prespliceosome stage PMID: 12101238
  39. synergism with transcriptional coactivators CBP and p300 PMID: 12527917
  40. role in c-H-ras alternative splicing regulation PMID: 12665590
  41. p68 is an important transcriptional regulator, functioning as a co-activator and/or co-repressor depending on the context of the promoter & the transcriptional complex. AA 1-478 of p68 can repress transcription as well as the full-length protein. PMID: 15298701
  42. there is a tightly controlled expression and nucleolar localization of p68 in keratinocytes in vitro and during skin repair in vivo that functionally contributes to keratinocyte proliferation and gene expression PMID: 15304501
  43. mechanism by which p68 may act as a tumour cosuppressor in governing p53 transcriptional activity PMID: 15660129
  44. data suggest that function(s) of p68 RNA helicase may be subjected to the regulation of multiple cell signal pathways PMID: 15927448
  45. In addition, it could be demonstrated that increasing the Tlk1 activity in HT1080 cells by forced Tlk1 overexpression leads to an increased phosphorylation of endogenous p68. PMID: 15950181
  46. Patient with chronic hepatitis C carrying DDX5 haplotypes are at an increased risk of developing advanced liver fibrosis. PMID: 16697732
  47. SUMO modification of the DEAD box protein p68 modulates its transcriptional activity and promotes its interaction with HDAC1 PMID: 17369852
  48. A mutant that carries mutations at the phosphorylation sites (Y593/595F) dramatically sensitizes TRAIL-resistant cells to TRAIL-induced apoptosis, suggesting a potential therapeutic strategy to overcome TRAIL resistance. PMID: 17384675
  49. The percentage correlation between Q-RT-PCR and microarray were 70% and 48% by using DDX5 and GAPDH as internal controls, respectively. PMID: 17540040
  50. p68/p72 may contribute to colon cancer formation by directly up-regulating proto-oncogenes and indirectly by down-regulating the growth suppressor p21(WAF1/CIP1). PMID: 17699760

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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.

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